Ligand binding to human prostaglandin E receptor EP4 at the lipid-bilayer interface

Prostaglandin E receptor EP4, a G-protein-coupled receptor, is involved in disorders such as cancer and autoimmune disease. Here, we report the crystal structure of human EP4 in complex with its antagonist ONO-AE3-208 and an inhibitory antibody at 3.2 Å resolution. The structure reveals that the ext...

Full description

Saved in:
Bibliographic Details
Published in:Nature chemical biology Vol. 15; no. 1; pp. 18 - 26
Main Authors: Toyoda, Yosuke, Morimoto, Kazushi, Suno, Ryoji, Horita, Shoichiro, Yamashita, Keitaro, Hirata, Kunio, Sekiguchi, Yusuke, Yasuda, Satoshi, Shiroishi, Mitsunori, Shimizu, Tomoko, Urushibata, Yuji, Kajiwara, Yuta, Inazumi, Tomoaki, Hotta, Yunhon, Asada, Hidetsugu, Nakane, Takanori, Shiimura, Yuki, Nakagita, Tomoya, Tsuge, Kyoshiro, Yoshida, Suguru, Kuribara, Tomoko, Hosoya, Takamitsu, Sugimoto, Yukihiko, Nomura, Norimichi, Sato, Miwa, Hirokawa, Takatsugu, Kinoshita, Masahiro, Murata, Takeshi, Takayama, Kiyoshi, Yamamoto, Masaki, Narumiya, Shuh, Iwata, So, Kobayashi, Takuya
Format: Journal Article
Language:English
Published: New York Nature Publishing Group US 01.01.2019
Nature Publishing Group
Subjects:
631/154/436
631/45/535
631/45/535/1266
631/92/287
Allosteric properties
Binding
Biochemical Engineering
Biochemistry
Bioorganic Chemistry
Cancer
Cell Biology
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Crystal structure
Docking
Drug delivery
Drug development
G protein-coupled receptors
Ligands
Lipid bilayers
Lipids
Prostaglandin E
Prostaglandin E2
Proteins
ISSN:1552-4450, 1552-4469, 1552-4469
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Abstract Prostaglandin E receptor EP4, a G-protein-coupled receptor, is involved in disorders such as cancer and autoimmune disease. Here, we report the crystal structure of human EP4 in complex with its antagonist ONO-AE3-208 and an inhibitory antibody at 3.2 Å resolution. The structure reveals that the extracellular surface is occluded by the extracellular loops and that the antagonist lies at the interface with the lipid bilayer, proximal to the highly conserved Arg316 residue in the seventh transmembrane domain. Functional and docking studies demonstrate that the natural agonist PGE 2 binds in a similar manner. This structural information also provides insight into the ligand entry pathway from the membrane bilayer to the EP4 binding pocket. Furthermore, the structure reveals that the antibody allosterically affects the ligand binding of EP4. These results should facilitate the design of new therapeutic drugs targeting both orthosteric and allosteric sites in this receptor family. The structure of human prostaglandin E receptor EP4 in complex with antagonist ONO-AE3-208 and a functional antibody reveals a ligand-binding site at the interface of the lipid bilayer that is unique among GPCRs.
AbstractList Prostaglandin E receptor EP4, a G-protein-coupled receptor, is involved in disorders such as cancer and autoimmune disease. Here, we report the crystal structure of human EP4 in complex with its antagonist ONO-AE3-208 and an inhibitory antibody at 3.2 Å resolution. The structure reveals that the extracellular surface is occluded by the extracellular loops and that the antagonist lies at the interface with the lipid bilayer, proximal to the highly conserved Arg316 residue in the seventh transmembrane domain. Functional and docking studies demonstrate that the natural agonist PGE 2 binds in a similar manner. This structural information also provides insight into the ligand entry pathway from the membrane bilayer to the EP4 binding pocket. Furthermore, the structure reveals that the antibody allosterically affects the ligand binding of EP4. These results should facilitate the design of new therapeutic drugs targeting both orthosteric and allosteric sites in this receptor family. The structure of human prostaglandin E receptor EP4 in complex with antagonist ONO-AE3-208 and a functional antibody reveals a ligand-binding site at the interface of the lipid bilayer that is unique among GPCRs.
Prostaglandin E receptor EP4, a G-protein-coupled receptor, is involved in disorders such as cancer and autoimmune disease. Here, we report the crystal structure of human EP4 in complex with its antagonist ONO-AE3-208 and an inhibitory antibody at 3.2 Å resolution. The structure reveals that the extracellular surface is occluded by the extracellular loops and that the antagonist lies at the interface with the lipid bilayer, proximal to the highly conserved Arg316 residue in the seventh transmembrane domain. Functional and docking studies demonstrate that the natural agonist PGE2 binds in a similar manner. This structural information also provides insight into the ligand entry pathway from the membrane bilayer to the EP4 binding pocket. Furthermore, the structure reveals that the antibody allosterically affects the ligand binding of EP4. These results should facilitate the design of new therapeutic drugs targeting both orthosteric and allosteric sites in this receptor family.Prostaglandin E receptor EP4, a G-protein-coupled receptor, is involved in disorders such as cancer and autoimmune disease. Here, we report the crystal structure of human EP4 in complex with its antagonist ONO-AE3-208 and an inhibitory antibody at 3.2 Å resolution. The structure reveals that the extracellular surface is occluded by the extracellular loops and that the antagonist lies at the interface with the lipid bilayer, proximal to the highly conserved Arg316 residue in the seventh transmembrane domain. Functional and docking studies demonstrate that the natural agonist PGE2 binds in a similar manner. This structural information also provides insight into the ligand entry pathway from the membrane bilayer to the EP4 binding pocket. Furthermore, the structure reveals that the antibody allosterically affects the ligand binding of EP4. These results should facilitate the design of new therapeutic drugs targeting both orthosteric and allosteric sites in this receptor family.
Prostaglandin E receptor EP4, a G-protein-coupled receptor, is involved in disorders such as cancer and autoimmune disease. Here, we report the crystal structure of human EP4 in complex with its antagonist ONO-AE3-208 and an inhibitory antibody at 3.2 Å resolution. The structure reveals that the extracellular surface is occluded by the extracellular loops and that the antagonist lies at the interface with the lipid bilayer, proximal to the highly conserved Arg316 residue in the seventh transmembrane domain. Functional and docking studies demonstrate that the natural agonist PGE2 binds in a similar manner. This structural information also provides insight into the ligand entry pathway from the membrane bilayer to the EP4 binding pocket. Furthermore, the structure reveals that the antibody allosterically affects the ligand binding of EP4. These results should facilitate the design of new therapeutic drugs targeting both orthosteric and allosteric sites in this receptor family.
Author Yoshida, Suguru
Hirata, Kunio
Kinoshita, Masahiro
Morimoto, Kazushi
Nakane, Takanori
Murata, Takeshi
Yamashita, Keitaro
Shimizu, Tomoko
Nomura, Norimichi
Toyoda, Yosuke
Takayama, Kiyoshi
Hotta, Yunhon
Kajiwara, Yuta
Sekiguchi, Yusuke
Urushibata, Yuji
Shiroishi, Mitsunori
Yasuda, Satoshi
Tsuge, Kyoshiro
Inazumi, Tomoaki
Shiimura, Yuki
Hosoya, Takamitsu
Narumiya, Shuh
Kobayashi, Takuya
Sato, Miwa
Kuribara, Tomoko
Sugimoto, Yukihiko
Hirokawa, Takatsugu
Yamamoto, Masaki
Asada, Hidetsugu
Iwata, So
Suno, Ryoji
Nakagita, Tomoya
Horita, Shoichiro
Author_xml – sequence: 1
  givenname: Yosuke
  orcidid: 0000-0002-2245-4666
  surname: Toyoda
  fullname: Toyoda, Yosuke
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, School of Medicine, Tsinghua University
– sequence: 2
  givenname: Kazushi
  orcidid: 0000-0001-7698-9378
  surname: Morimoto
  fullname: Morimoto, Kazushi
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 3
  givenname: Ryoji
  surname: Suno
  fullname: Suno, Ryoji
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 4
  givenname: Shoichiro
  surname: Horita
  fullname: Horita, Shoichiro
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 5
  givenname: Keitaro
  orcidid: 0000-0002-5442-7582
  surname: Yamashita
  fullname: Yamashita, Keitaro
  organization: RIKEN SPring-8 Center, Sayo-cho, Sayo-gun
– sequence: 6
  givenname: Kunio
  surname: Hirata
  fullname: Hirata, Kunio
  organization: RIKEN SPring-8 Center, Sayo-cho, Sayo-gun
– sequence: 7
  givenname: Yusuke
  surname: Sekiguchi
  fullname: Sekiguchi, Yusuke
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 8
  givenname: Satoshi
  orcidid: 0000-0003-3555-1083
  surname: Yasuda
  fullname: Yasuda, Satoshi
  organization: Department of Chemistry, Graduate School of Science, Chiba University, Inage, Institute of Advanced Energy, Kyoto University
– sequence: 9
  givenname: Mitsunori
  surname: Shiroishi
  fullname: Shiroishi, Mitsunori
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Japan Science and Technology Agency (JST), Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 10
  givenname: Tomoko
  surname: Shimizu
  fullname: Shimizu, Tomoko
  organization: NB Health Laboratory Co. Ltd., Kita Ward Sapporo City
– sequence: 11
  givenname: Yuji
  surname: Urushibata
  fullname: Urushibata, Yuji
  organization: NB Health Laboratory Co. Ltd., Kita Ward Sapporo City
– sequence: 12
  givenname: Yuta
  surname: Kajiwara
  fullname: Kajiwara, Yuta
  organization: Graduate School of Energy Science, Kyoto University, Molecular Profiling Research Center for Drug Discovery (MOLPROF), National Institute of Advanced Industrial Science and Technology (AIST)
– sequence: 13
  givenname: Tomoaki
  surname: Inazumi
  fullname: Inazumi, Tomoaki
  organization: Department of Pharmaceutical Biochemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University, Oe-Honmachi
– sequence: 14
  givenname: Yunhon
  orcidid: 0000-0003-4062-1103
  surname: Hotta
  fullname: Hotta, Yunhon
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 15
  givenname: Hidetsugu
  orcidid: 0000-0001-6255-4728
  surname: Asada
  fullname: Asada, Hidetsugu
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, JST, the Strategic Basic Research Program, Membrane Protein Crystallography Project
– sequence: 16
  givenname: Takanori
  orcidid: 0000-0003-2697-2767
  surname: Nakane
  fullname: Nakane, Takanori
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 17
  givenname: Yuki
  surname: Shiimura
  fullname: Shiimura, Yuki
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, JST, the Strategic Basic Research Program, Membrane Protein Crystallography Project
– sequence: 18
  givenname: Tomoya
  orcidid: 0000-0002-0542-8650
  surname: Nakagita
  fullname: Nakagita, Tomoya
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 19
  givenname: Kyoshiro
  orcidid: 0000-0001-9419-7331
  surname: Tsuge
  fullname: Tsuge, Kyoshiro
  organization: Department of Pharmaceutical Biochemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University, Oe-Honmachi
– sequence: 20
  givenname: Suguru
  orcidid: 0000-0001-5888-9330
  surname: Yoshida
  fullname: Yoshida, Suguru
  organization: Laboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, Chiyoda-ku
– sequence: 21
  givenname: Tomoko
  surname: Kuribara
  fullname: Kuribara, Tomoko
  organization: Laboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, Chiyoda-ku
– sequence: 22
  givenname: Takamitsu
  orcidid: 0000-0002-7270-351X
  surname: Hosoya
  fullname: Hosoya, Takamitsu
  organization: Japan Science and Technology Agency (JST), Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku, Laboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, Chiyoda-ku
– sequence: 23
  givenname: Yukihiko
  orcidid: 0000-0001-6973-932X
  surname: Sugimoto
  fullname: Sugimoto, Yukihiko
  organization: Department of Pharmaceutical Biochemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University, Oe-Honmachi, Japan Agency for Medical Research and Development (AMED), Core Research for Evolutional Science and Technology (CREST), Chiyoda-ku
– sequence: 24
  givenname: Norimichi
  orcidid: 0000-0002-6330-2239
  surname: Nomura
  fullname: Nomura, Norimichi
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, JST, the Strategic Basic Research Program, Membrane Protein Crystallography Project
– sequence: 25
  givenname: Miwa
  surname: Sato
  fullname: Sato, Miwa
  organization: Biomedical Department, Mitsui Knowledge Industry Co., Minato-ku
– sequence: 26
  givenname: Takatsugu
  surname: Hirokawa
  fullname: Hirokawa, Takatsugu
  organization: Japan Science and Technology Agency (JST), Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku, Molecular Profiling Research Center for Drug Discovery (MOLPROF), National Institute of Advanced Industrial Science and Technology (AIST), Division of Biomedical Science, Faculty of Medicine, University of Tsukuba
– sequence: 27
  givenname: Masahiro
  orcidid: 0000-0001-8060-045X
  surname: Kinoshita
  fullname: Kinoshita, Masahiro
  organization: Institute of Advanced Energy, Kyoto University
– sequence: 28
  givenname: Takeshi
  orcidid: 0000-0002-5748-4670
  surname: Murata
  fullname: Murata, Takeshi
  organization: Department of Chemistry, Graduate School of Science, Chiba University, Inage, Japan Science and Technology Agency (JST), Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 29
  givenname: Kiyoshi
  surname: Takayama
  fullname: Takayama, Kiyoshi
  organization: NB Health Laboratory Co. Ltd., Kita Ward Sapporo City
– sequence: 30
  givenname: Masaki
  surname: Yamamoto
  fullname: Yamamoto, Masaki
  organization: RIKEN SPring-8 Center, Sayo-cho, Sayo-gun, Japan Science and Technology Agency (JST), Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku
– sequence: 31
  givenname: Shuh
  surname: Narumiya
  fullname: Narumiya, Shuh
  email: s.naru@mfour.med.kyoto-u.ac.jp
  organization: Japan Agency for Medical Research and Development (AMED), Core Research for Evolutional Science and Technology (CREST), Chiyoda-ku, Medical Innovation Center, Kyoto University Graduate School of Medicine, Sakyo-ku
– sequence: 32
  givenname: So
  orcidid: 0000-0003-1735-2937
  surname: Iwata
  fullname: Iwata, So
  email: s.iwata@mfour.med.kyoto-u.ac.jp
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, RIKEN SPring-8 Center, Sayo-cho, Sayo-gun, JST, the Strategic Basic Research Program, Membrane Protein Crystallography Project
– sequence: 33
  givenname: Takuya
  surname: Kobayashi
  fullname: Kobayashi, Takuya
  email: kobayashi.takuya.4r@kyoto-u.ac.jp
  organization: Department of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Japan Science and Technology Agency (JST), Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku, JST, the Strategic Basic Research Program, Membrane Protein Crystallography Project, Japan Agency for Medical Research and Development (AMED), Core Research for Evolutional Science and Technology (CREST), Chiyoda-ku
BookMark eNp9kF9LwzAUxYMouE0_gG8BX3ypJk3SpY8y5h8YKKjPIUnTLqNLa5I-7NubUlEY6MPl3oTfyT05c3DqOmcAuMLoFiPC7wLFjJcZwjwVwRk5ATPMWJ5RWpSnPzND52Aewg4hUhSYz8DbxjbSVVBZV1nXwNjB7bCXDva-C1E2rRzv4Rp6o00fOw_XrxTKCOPWwNb2tsqUbeXBeGhdNL6W2lyAs1q2wVx-9wX4eFi_r56yzcvj8-p-k2lCWcxyplle46rmpuJ5vaSkQprSdFBES0XzZHcpkZSkLlPHGiNcKqYQUQZXTJEFuJneTV4_BxOi2NugTZs8m24IIse05IxSXib0-gjddYN3yV2iWFpV8GKk8ETp9PngTS16b_fSHwRGYoxZTDGLFLMYYxYkaZZHGm2jjLZz0Uvb_qvMJ2VIW1xj_K-nv0VfNbaSfQ
CitedBy_id crossref_primary_10_1038_s41467_023_43922_8
crossref_primary_10_1038_s41598_022_17920_7
crossref_primary_10_1016_j_tibs_2019_02_001
crossref_primary_10_1038_s41589_018_0171_8
crossref_primary_10_1016_j_molstruc_2022_132730
crossref_primary_10_1007_s10557_020_07031_8
crossref_primary_10_7554_eLife_58464
crossref_primary_10_1016_j_csbj_2023_07_007
crossref_primary_10_1038_s41589_024_01620_6
crossref_primary_10_3390_ijms23158775
crossref_primary_10_3390_biom11070936
crossref_primary_10_1016_j_pep_2019_105545
crossref_primary_10_1038_s41594_021_00634_1
crossref_primary_10_1038_s41598_020_76277_x
crossref_primary_10_1038_s41596_019_0259_y
crossref_primary_10_1186_s12860_019_0212_5
crossref_primary_10_1016_j_str_2020_11_007
crossref_primary_10_1016_j_immuni_2021_06_001
crossref_primary_10_1073_pnas_2423840122
crossref_primary_10_1111_febs_15128
crossref_primary_10_1038_s41467_023_43506_6
crossref_primary_10_1038_s41467_022_33880_y
crossref_primary_10_1186_s12915_025_02200_3
crossref_primary_10_1038_s41467_020_20221_0
crossref_primary_10_1002_pro_4404
crossref_primary_10_1124_mol_119_118372
crossref_primary_10_1038_s41422_021_00552_3
crossref_primary_10_1002_pro_4520
crossref_primary_10_1186_s12964_024_01851_z
crossref_primary_10_1073_pnas_2102813118
crossref_primary_10_1016_j_bmc_2024_117653
crossref_primary_10_1016_j_fsi_2024_110108
crossref_primary_10_1016_j_molliq_2019_112403
crossref_primary_10_1038_s41556_021_00708_8
crossref_primary_10_1038_s41589_018_0178_1
crossref_primary_10_3390_ph15010012
crossref_primary_10_1016_j_jcis_2024_03_055
crossref_primary_10_1016_j_molcel_2025_02_030
crossref_primary_10_1016_j_bioorg_2025_109005
crossref_primary_10_1124_pr_120_019331
crossref_primary_10_15252_emmm_202012798
crossref_primary_10_3389_fimmu_2019_02156
crossref_primary_10_1111_jpi_12952
crossref_primary_10_1124_pr_119_017863
crossref_primary_10_1111_cbdd_70132
crossref_primary_10_1360_nso_20240015
crossref_primary_10_1038_s41596_021_00660_9
crossref_primary_10_1080_14712598_2020_1745770
crossref_primary_10_3390_ijms25136876
crossref_primary_10_1073_pnas_2216329120
crossref_primary_10_1038_s41467_023_43601_8
crossref_primary_10_1002_pro_4425
crossref_primary_10_1007_s11356_022_20108_1
crossref_primary_10_1007_s12551_020_00678_5
crossref_primary_10_1111_cas_14247
crossref_primary_10_1371_journal_pone_0320114
crossref_primary_10_1038_s41597_020_00729_2
crossref_primary_10_1194_jlr_R120000800
crossref_primary_10_3390_biom12010099
crossref_primary_10_1016_j_biopha_2021_111675
crossref_primary_10_1016_j_str_2021_02_003
crossref_primary_10_1038_s41467_023_39310_x
crossref_primary_10_1016_j_ejphar_2024_176904
crossref_primary_10_1038_s41467_020_17554_1
crossref_primary_10_1111_bph_17379
crossref_primary_10_1093_intimm_dxz021
crossref_primary_10_1016_j_sbi_2019_02_010
crossref_primary_10_1038_s42256_025_00982_3
Cites_doi 10.1107/S0907444909052925
10.1038/ng.2686
10.1107/S0907444913012274
10.1021/acs.jpcb.7b02997
10.1016/j.clinthera.2016.02.019
10.1038/nrd.2017.91
10.1124/jpet.109.156398
10.1107/S2059798318004576
10.1038/nature20613
10.1074/jbc.272.24.15154
10.1074/jbc.M207420200
10.1016/j.cell.2015.06.002
10.1152/physrev.1999.79.4.1193
10.3797/scipharm.1106-24
10.1016/j.jmb.2007.05.022
10.1016/j.drudis.2016.08.003
10.1126/science.1215904
10.1107/S0021889811041768
10.1038/nature22363
10.1124/mol.51.1.61
10.1111/jvim.13948
10.1038/nprot.2009.31
10.1186/1475-2859-11-78
10.1016/j.tibs.2014.03.002
10.1021/ci800324m
10.1016/j.tips.2015.09.005
10.1038/nature13494
10.1107/S0907444909047337
10.1126/science.289.5480.739
10.1124/mol.54.3.584
10.1371/journal.pgen.0030058
10.1124/mol.112.080473
10.1124/pr.112.007195
10.1016/S1043-9471(05)80049-7
10.1017/S0033583515000153
10.1107/S0108767307043930
10.1042/bj20021429
10.1038/nature11896
10.1002/pro.3035
10.1063/1.4952941
10.1021/acs.jctc.5b00864
10.1016/S0014-2999(98)00522-6
10.1073/pnas.0510562103
10.1016/j.ejphar.2015.02.021
10.1186/2051-1426-3-S2-P350
10.1107/S0907444910007493
10.1038/nmeth.2172
10.1021/cr200010h
10.1038/nm.1968
10.1021/jm050540c
10.1038/srep22639
10.1172/JCI0214459
10.1038/nature22309
10.1107/S0021889807021206
10.1038/ng.978
10.1124/mol.105.017749
ContentType Journal Article
Copyright Springer Nature America, Inc. 2018
Copyright Nature Publishing Group Jan 2019
Copyright_xml – notice: Springer Nature America, Inc. 2018
– notice: Copyright Nature Publishing Group Jan 2019
DBID AAYXX
CITATION
3V.
7QL
7QP
7QR
7TK
7TM
7U9
7X7
7XB
88A
88E
88I
8AO
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
ABJCF
ABUWG
AEUYN
AFKRA
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
BKSAR
C1K
CCPQU
D1I
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
H94
HCIFZ
K9.
KB.
LK8
M0S
M1P
M2P
M7N
M7P
P64
PCBAR
PDBOC
PHGZM
PHGZT
PJZUB
PKEHL
PPXIY
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
Q9U
RC3
7X8
DOI 10.1038/s41589-018-0131-3
DatabaseName CrossRef
ProQuest Central (Corporate)
Bacteriology Abstracts (Microbiology B)
Calcium & Calcified Tissue Abstracts
Chemoreception Abstracts
Neurosciences Abstracts
Nucleic Acids Abstracts
Virology and AIDS Abstracts
ProQuest Health & Medical Collection (NC LIVE)
ProQuest Central (purchase pre-March 2016)
Biology Database (Alumni Edition)
Medical Database (Alumni Edition)
Science Database (Alumni Edition)
ProQuest Pharma Collection
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
Materials Science & Engineering Collection
ProQuest Central (Alumni)
ProQuest One Sustainability
ProQuest Central UK/Ireland
ProQuest Central Essentials
ProQuest Biological Science Collection
ProQuest Central
Technology collection
ProQuest Natural Science Collection
Earth, Atmospheric & Aquatic Science Collection
Environmental Sciences and Pollution Management
ProQuest One Community College
ProQuest Materials Science Collection
ProQuest Central
Engineering Research Database
Proquest Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
AIDS and Cancer Research Abstracts
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
Materials Science Database
Biological Sciences
ProQuest Health & Medical Collection
Medical Database
ProQuest Science Database (NC LIVE)
Algology Mycology and Protozoology Abstracts (Microbiology C)
ProQuest Biological Science Database (NC LIVE)
Biotechnology and BioEngineering Abstracts
Earth, Atmospheric & Aquatic Science Database
Materials Science Collection
ProQuest Central Premium
ProQuest One Academic (New)
ProQuest Health & Medical Research Collection
ProQuest One Academic Middle East (New)
ProQuest One Health & Nursing
ProQuest One Academic Eastern Edition (DO NOT USE)
One Applied & Life Sciences
ProQuest One Academic (retired)
ProQuest One Academic UKI Edition
ProQuest Central China
ProQuest Central Basic
Genetics Abstracts
MEDLINE - Academic
DatabaseTitle CrossRef
ProQuest Central Student
ProQuest Central Essentials
Nucleic Acids Abstracts
SciTech Premium Collection
ProQuest Central China
Environmental Sciences and Pollution Management
ProQuest One Applied & Life Sciences
ProQuest One Sustainability
Health Research Premium Collection
Natural Science Collection
Health & Medical Research Collection
Biological Science Collection
Chemoreception Abstracts
ProQuest Central (New)
ProQuest Medical Library (Alumni)
Virology and AIDS Abstracts
ProQuest Science Journals (Alumni Edition)
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
Earth, Atmospheric & Aquatic Science Database
ProQuest Hospital Collection
ProQuest Technology Collection
Health Research Premium Collection (Alumni)
Biological Science Database
Neurosciences Abstracts
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
ProQuest Health & Medical Complete
ProQuest One Academic UKI Edition
Engineering Research Database
ProQuest One Academic
Calcium & Calcified Tissue Abstracts
ProQuest One Academic (New)
Technology Collection
Technology Research Database
ProQuest One Academic Middle East (New)
Materials Science Collection
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest One Health & Nursing
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Biology Journals (Alumni Edition)
ProQuest Central
Earth, Atmospheric & Aquatic Science Collection
ProQuest Health & Medical Research Collection
Genetics Abstracts
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
AIDS and Cancer Research Abstracts
Materials Science Database
ProQuest Materials Science Collection
ProQuest Central Basic
ProQuest Science Journals
ProQuest SciTech Collection
ProQuest Medical Library
Materials Science & Engineering Collection
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic
ProQuest Central Student
Database_xml – sequence: 1
  dbid: BENPR
  name: ProQuest Central
  url: https://www.proquest.com/central
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Anatomy & Physiology
Chemistry
EISSN 1552-4469
EndPage 26
ExternalDocumentID 10_1038_s41589_018_0131_3
GroupedDBID ---
0R~
123
29M
39C
3V.
4.4
53G
5BI
70F
7X7
88A
88E
88I
8AO
8FE
8FG
8FH
8FI
8FJ
8R4
8R5
AAEEF
AARCD
AAYZH
AAZLF
ABAWZ
ABDBF
ABJCF
ABJNI
ABLJU
ABUWG
ACBWK
ACGFS
ACGOD
ACIWK
ACPRK
ACUHS
ADBBV
AENEX
AEUYN
AFANA
AFBBN
AFKRA
AFRAH
AFSHS
AGAYW
AGHTU
AHBCP
AHMBA
AHOSX
AHSBF
AIBTJ
ALFFA
ALIPV
ALMA_UNASSIGNED_HOLDINGS
ARMCB
ASPBG
AVWKF
AXYYD
AZFZN
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
BKKNO
BKSAR
BPHCQ
BVXVI
CCPQU
CS3
CZ9
D1I
DB5
DU5
DWQXO
EBS
EE.
EJD
EMOBN
ESX
EXGXG
F5P
FEDTE
FQGFK
FSGXE
FYUFA
GNUQQ
HCIFZ
HMCUK
HVGLF
HZ~
KB.
KC.
LK5
LK8
M0L
M1P
M2P
M7P
M7R
NACWA
NNMJJ
O9-
ODYON
P2P
PCBAR
PDBOC
PQQKQ
PROAC
PSQYO
Q2X
RNT
RNTTT
SHXYY
SIXXV
SJN
SNYQT
SOJ
SV3
TAOOD
TBHMF
TDRGL
TSG
TUS
UKHRP
~8M
AAYXX
AGSTI
ALPWD
ATHPR
CITATION
7QL
7QP
7QR
7TK
7TM
7U9
7XB
8FD
8FK
ABFSG
ACSTC
AEZWR
AFHIU
AHWEU
AIXLP
C1K
FR3
H94
K9.
M7N
P64
PHGZM
PHGZT
PJZUB
PKEHL
PPXIY
PQEST
PQGLB
PQUKI
PRINS
Q9U
RC3
7X8
PUEGO
ID FETCH-LOGICAL-c345t-25c52f1df8ed82f743d0c44ed8b3cab424457a0aa3f97a01c1019b5b03be1d5b3
IEDL.DBID KB.
ISICitedReferencesCount 95
ISICitedReferencesURI http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000452634100011&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN 1552-4450
1552-4469
IngestDate Thu Oct 02 16:36:31 EDT 2025
Fri Oct 03 06:20:23 EDT 2025
Sat Nov 29 02:45:18 EST 2025
Tue Nov 18 22:40:04 EST 2025
Fri Feb 21 02:39:33 EST 2025
IsPeerReviewed true
IsScholarly true
Issue 1
Language English
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c345t-25c52f1df8ed82f743d0c44ed8b3cab424457a0aa3f97a01c1019b5b03be1d5b3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
ORCID 0000-0002-2245-4666
0000-0001-6973-932X
0000-0003-2697-2767
0000-0002-7270-351X
0000-0001-7698-9378
0000-0002-5442-7582
0000-0001-5888-9330
0000-0002-5748-4670
0000-0001-8060-045X
0000-0003-3555-1083
0000-0001-9419-7331
0000-0001-6255-4728
0000-0003-4062-1103
0000-0003-1735-2937
0000-0002-0542-8650
0000-0002-6330-2239
PQID 2154246869
PQPubID 29034
PageCount 9
ParticipantIDs proquest_miscellaneous_2149854489
proquest_journals_2154246869
crossref_primary_10_1038_s41589_018_0131_3
crossref_citationtrail_10_1038_s41589_018_0131_3
springer_journals_10_1038_s41589_018_0131_3
PublicationCentury 2000
PublicationDate 2019-01-01
PublicationDateYYYYMMDD 2019-01-01
PublicationDate_xml – month: 01
  year: 2019
  text: 2019-01-01
  day: 01
PublicationDecade 2010
PublicationPlace New York
PublicationPlace_xml – name: New York
– name: Cambridge
PublicationTitle Nature chemical biology
PublicationTitleAbbrev Nat Chem Biol
PublicationYear 2019
Publisher Nature Publishing Group US
Nature Publishing Group
Publisher_xml – name: Nature Publishing Group US
– name: Nature Publishing Group
References Shao (CR27) 2016; 540
Buchanan (CR3) 2006; 103
Stillman, Audoly, Breyer (CR15) 1998; 357
Sheldrick (CR55) 2008; 64
Zare, Madadkar-Sobhani, Dastmalchi, Mahmoudian (CR40) 2011; 79
Ballesteros, Weinstein (CR20) 1995; 25
Inoue (CR45) 2012; 9
Krissinel, Henrick (CR57) 2007; 372
Adams (CR54) 2010; 66
Katritch (CR21) 2014; 39
Thorn, Sheldrick (CR56) 2011; 44
Sherman, Day, Jacobson, Friesner, Farid (CR59) 2006; 49
Caffrey, Cherezov (CR47) 2009; 4
Yokoyama, Iwatsubo, Umemura, Fujita, Ishikawa (CR4) 2013; 65
Palczewski (CR29) 2000; 289
McCoy (CR52) 2007; 40
Stitham, Stojanovic, Merenick, O’Hara, Hwa (CR35) 2003; 278
Kobayashi (CR14) 1997; 272
Kabashima (CR23) 2002; 109
Ward (CR10) 2016; 38
Foadi (CR51) 2013; 69
Margan, Borota, Mracec, Mracec (CR39) 2012; 57
Harder (CR60) 2016; 12
Hutchings, Koglin, Olson, Marshall (CR41) 2017; 16
Kedzie, Donello, Krauss, Regan, Gil (CR33) 1998; 54
Halgren (CR58) 2009; 49
Case (CR61) 2010
Venkatakrishnan (CR24) 2013; 494
Hanson (CR25) 2012; 335
Libioulle (CR6) 2007; 3
Vaidehi, Grisshammer, Tate (CR18) 2016; 37
Neuschäfer-Rube, Engemaier, Koch, Böer, Püschel (CR36) 2003; 371
Zhang (CR43) 2017; 546
Srivastava (CR28) 2014; 513
Stanley, Pardo, Fabritiis (CR31) 2016; 6
Audoly, Breyer (CR34) 1997; 51
Nomura (CR46) 2016; 25
Funk, Furci, Moran, Fitzgerald (CR37) 1993; 44
Ueno (CR48) 2016; 1741
Shiroishi (CR17) 2012; 11
Natarajan, Hata, Hamm, Zent, Breyer (CR38) 2013; 83
Narumiya, Sugimoto, Ushikubi (CR16) 1999; 79
Fujino, Regan (CR2) 2006; 69
Rausch-Derra, Huebner, Wofford, Rhodes (CR12) 2016; 30
Cheng (CR42) 2017; 545
Hinds (CR8) 2013; 45
Hirata, Narumiya (CR1) 2011; 111
Bao (CR13) 2015; 3
Yasuda (CR19) 2017; 121
Kabsch (CR50) 2010; 66
Kappel, Miao, McCammon (CR30) 2015; 48
Shi (CR7) 2011; 43
Chrencik (CR26) 2015; 161
Markovič, Jakopin, Dolenc, Mlinarič-Raščan (CR9) 2017; 22
Yao (CR5) 2009; 15
CR22
Mutoh (CR32) 2002; 62
Emsley, Lohkamp, Scott, Cowtan (CR53) 2010; 66
Watanabe (CR11) 2015; 754
Yamashita, Hirata, Yamamoto (CR49) 2018; 74
Leduc (CR44) 2009; 331
Z Shao (131_CR27) 2016; 540
D Margan (131_CR39) 2012; 57
W Kabsch (131_CR50) 2010; 66
BA Stillman (131_CR15) 1998; 357
K Kabashima (131_CR23) 2002; 109
M Caffrey (131_CR47) 2009; 4
X Bao (131_CR13) 2015; 3
JA Ballesteros (131_CR20) 1995; 25
F Neuschäfer-Rube (131_CR36) 2003; 371
RKY Cheng (131_CR42) 2017; 545
C Libioulle (131_CR6) 2007; 3
A Thorn (131_CR56) 2011; 44
AJ McCoy (131_CR52) 2007; 40
K Palczewski (131_CR29) 2000; 289
G Ueno (131_CR48) 2016; 1741
CD Funk (131_CR37) 1993; 44
E Harder (131_CR60) 2016; 12
PD Adams (131_CR54) 2010; 66
L Audoly (131_CR34) 1997; 51
131_CR22
N Stanley (131_CR31) 2016; 6
L Rausch-Derra (131_CR12) 2016; 30
MA Hanson (131_CR25) 2012; 335
M Mutoh (131_CR32) 2002; 62
AJ Venkatakrishnan (131_CR24) 2013; 494
B Zare (131_CR40) 2011; 79
T Hirata (131_CR1) 2011; 111
Y Watanabe (131_CR11) 2015; 754
T Markovič (131_CR9) 2017; 22
K Yamashita (131_CR49) 2018; 74
K Kappel (131_CR30) 2015; 48
E Krissinel (131_CR57) 2007; 372
CJ Hutchings (131_CR41) 2017; 16
DA Case (131_CR61) 2010
Y Nomura (131_CR46) 2016; 25
P Emsley (131_CR53) 2010; 66
J Foadi (131_CR51) 2013; 69
JE Chrencik (131_CR26) 2015; 161
KM Kedzie (131_CR33) 1998; 54
C Yao (131_CR5) 2009; 15
A Srivastava (131_CR28) 2014; 513
H Fujino (131_CR2) 2006; 69
DA Hinds (131_CR8) 2013; 45
A Inoue (131_CR45) 2012; 9
FG Buchanan (131_CR3) 2006; 103
J Stitham (131_CR35) 2003; 278
N Vaidehi (131_CR18) 2016; 37
C Natarajan (131_CR38) 2013; 83
W Sherman (131_CR59) 2006; 49
H Zhang (131_CR43) 2017; 546
T Kobayashi (131_CR14) 1997; 272
V Katritch (131_CR21) 2014; 39
CL Ward (131_CR10) 2016; 38
TA Halgren (131_CR58) 2009; 49
Y Shi (131_CR7) 2011; 43
S Narumiya (131_CR16) 1999; 79
M Leduc (131_CR44) 2009; 331
S Yasuda (131_CR19) 2017; 121
GM Sheldrick (131_CR55) 2008; 64
U Yokoyama (131_CR4) 2013; 65
M Shiroishi (131_CR17) 2012; 11
References_xml – volume: 66
  start-page: 213
  year: 2010
  end-page: 221
  ident: CR54
  article-title: PHENIX: a comprehensive Python-based system for macromolecular structure solution
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444909052925
– ident: CR22
– volume: 45
  start-page: 907
  year: 2013
  end-page: 911
  ident: CR8
  article-title: A genome-wide association meta-analysis of self-reported allergy identifies shared and allergy-specific susceptibility loci
  publication-title: Nat. Genet.
  doi: 10.1038/ng.2686
– volume: 69
  start-page: 1617
  year: 2013
  end-page: 1632
  ident: CR51
  article-title: Clustering procedures for the optimal selection of data sets from multiple crystals in macromolecular crystallography
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444913012274
– volume: 121
  start-page: 6341
  year: 2017
  end-page: 6350
  ident: CR19
  article-title: Hot-spot residues to be mutated common in G protein-coupled receptors of class A: identification of thermostabilizing mutations followed by determination of three-dimensional structures for two example receptors
  publication-title: J. Phys. Chem. B
  doi: 10.1021/acs.jpcb.7b02997
– volume: 38
  start-page: 1109
  year: 2016
  end-page: 1121
  ident: CR10
  article-title: First clinical experience with ONO-4232: a randomized, double-blind, placebo-controlled healthy volunteer study of a novel lusitropic agent for acutely decompensated heart failure
  publication-title: Clin. Ther.
  doi: 10.1016/j.clinthera.2016.02.019
– volume: 16
  start-page: 787
  year: 2017
  end-page: 810
  ident: CR41
  article-title: Opportunities for therapeutic antibodies directed at G-protein-coupled receptors
  publication-title: Nat. Rev. Drug. Discov.
  doi: 10.1038/nrd.2017.91
– volume: 331
  start-page: 297
  year: 2009
  end-page: 307
  ident: CR44
  article-title: Functional selectivity of natural and synthetic prostaglandin EP4 receptor ligands
  publication-title: J. Pharmacol. Exp. Ther.
  doi: 10.1124/jpet.109.156398
– volume: 74
  start-page: 441
  year: 2018
  end-page: 449
  ident: CR49
  article-title: KAMO: towards automated data processing for microcrystals.
  publication-title: Acta Crystallogr. D Struct. Biol.
  doi: 10.1107/S2059798318004576
– volume: 540
  start-page: 602
  year: 2016
  end-page: 606
  ident: CR27
  article-title: High-resolution crystal structure of the human CB1 cannabinoid receptor
  publication-title: Nature
  doi: 10.1038/nature20613
– volume: 272
  start-page: 15154
  year: 1997
  end-page: 15160
  ident: CR14
  article-title: Identification of domains conferring ligand binding specificity to the prostanoid receptor. Studies on chimeric prostacyclin/prostaglandin D receptors
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.272.24.15154
– volume: 278
  start-page: 4250
  year: 2003
  end-page: 4257
  ident: CR35
  article-title: The unique ligand-binding pocket for the human prostacyclin receptor. Site-directed mutagenesis and molecular modeling
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M207420200
– volume: 161
  start-page: 1633
  year: 2015
  end-page: 1643
  ident: CR26
  article-title: Crystal structure of antagonist bound human lysophosphatidic acid receptor 1
  publication-title: Cell
  doi: 10.1016/j.cell.2015.06.002
– volume: 57
  start-page: 39
  year: 2012
  end-page: 44
  ident: CR39
  article-title: 3D homology model of the human prostaglandin E2 receptor EP4 subtype
  publication-title: Rev. Roum. Chim.
– volume: 79
  start-page: 1193
  year: 1999
  end-page: 1226
  ident: CR16
  article-title: Prostanoid receptors: structures, properties, and functions
  publication-title: Physiol. Rev.
  doi: 10.1152/physrev.1999.79.4.1193
– volume: 79
  start-page: 793
  year: 2011
  end-page: 816
  ident: CR40
  article-title: Prediction of the human EP1 receptor binding site by homology modeling and molecular dynamics simulation
  publication-title: Sci. Pharm.
  doi: 10.3797/scipharm.1106-24
– volume: 372
  start-page: 774
  year: 2007
  end-page: 797
  ident: CR57
  article-title: Inference of macromolecular assemblies from crystalline state
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2007.05.022
– volume: 22
  start-page: 57
  year: 2017
  end-page: 71
  ident: CR9
  article-title: Structural features of subtype-selective EP receptor modulators
  publication-title: Drug Discov. Today
  doi: 10.1016/j.drudis.2016.08.003
– volume: 335
  start-page: 851
  year: 2012
  end-page: 855
  ident: CR25
  article-title: Crystal structure of a lipid G protein-coupled receptor
  publication-title: Science
  doi: 10.1126/science.1215904
– volume: 44
  start-page: 1285
  year: 2011
  end-page: 1287
  ident: CR56
  article-title: ANODE: anomalous and heavy-atom density calculation
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889811041768
– volume: 546
  start-page: 259
  year: 2017
  end-page: 264
  ident: CR43
  article-title: Structure of the full-length glucagon class B G-protein-coupled receptor
  publication-title: Nature
  doi: 10.1038/nature22363
– volume: 51
  start-page: 61
  year: 1997
  end-page: 68
  ident: CR34
  article-title: Substitution of charged amino acid residues in transmembrane regions 6 and 7 affect ligand binding and signal transduction of the prostaglandin EP3 receptor
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.51.1.61
– volume: 30
  start-page: 756
  year: 2016
  end-page: 763
  ident: CR12
  article-title: A prospective, randomized, masked, placebo-controlled multisite clinical study of grapiprant, an EP4 prostaglandin receptor antagonist (PRA), in dogs with osteoarthritis
  publication-title: J. Vet. Intern. Med.
  doi: 10.1111/jvim.13948
– volume: 4
  start-page: 706
  year: 2009
  end-page: 731
  ident: CR47
  article-title: Crystallizing membrane proteins using lipidic mesophases
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2009.31
– volume: 11
  start-page: 78
  year: 2012
  ident: CR17
  article-title: Platform for the rapid construction and evaluation of GPCRs for crystallography in
  publication-title: Microb. Cell. Fact.
  doi: 10.1186/1475-2859-11-78
– volume: 39
  start-page: 233
  year: 2014
  end-page: 244
  ident: CR21
  article-title: Allosteric sodium in class A GPCR signaling
  publication-title: Trends. Biochem. Sci.
  doi: 10.1016/j.tibs.2014.03.002
– volume: 49
  start-page: 377
  year: 2009
  end-page: 389
  ident: CR58
  article-title: Identifying and characterizing binding sites and assessing druggability
  publication-title: J. Chem. Inf. Model.
  doi: 10.1021/ci800324m
– year: 2010
  ident: CR61
  publication-title: AMBER 11
– volume: 37
  start-page: 37
  year: 2016
  end-page: 46
  ident: CR18
  article-title: How can mutations thermostabilize G-protein-coupled receptors?
  publication-title: Trends Pharmacol. Sci.
  doi: 10.1016/j.tips.2015.09.005
– volume: 513
  start-page: 124
  year: 2014
  end-page: 127
  ident: CR28
  article-title: High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875
  publication-title: Nature
  doi: 10.1038/nature13494
– volume: 62
  start-page: 28
  year: 2002
  end-page: 32
  ident: CR32
  article-title: Involvement of prostaglandin E receptor subtype EP in colon carcinogenesis
  publication-title: Cancer Res.
– volume: 66
  start-page: 125
  year: 2010
  end-page: 132
  ident: CR50
  article-title: XDS.
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444909047337
– volume: 289
  start-page: 739
  year: 2000
  end-page: 745
  ident: CR29
  article-title: Crystal structure of rhodopsin: a G protein-coupled receptor
  publication-title: Science
  doi: 10.1126/science.289.5480.739
– volume: 54
  start-page: 584
  year: 1998
  end-page: 590
  ident: CR33
  article-title: A single amino-acid substitution in the EP2 prostaglandin receptor confers responsiveness to prostacyclin analogs
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.54.3.584
– volume: 3
  start-page: e58
  year: 2007
  ident: CR6
  article-title: Novel Crohn disease locus identified by genome-wide association maps to a gene desert on 5p13.1 and modulates expression of PTGER4
  publication-title: PLoS. Genet.
  doi: 10.1371/journal.pgen.0030058
– volume: 83
  start-page: 206
  year: 2013
  end-page: 216
  ident: CR38
  article-title: Extracellular loop II modulates GTP sensitivity of the prostaglandin EP3 receptor
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.112.080473
– volume: 65
  start-page: 1010
  year: 2013
  end-page: 1052
  ident: CR4
  article-title: The prostanoid EP4 receptor and its signaling pathway
  publication-title: Pharmacol. Rev.
  doi: 10.1124/pr.112.007195
– volume: 25
  start-page: 366
  year: 1995
  end-page: 428
  ident: CR20
  article-title: Integrated methods for the construction of three dimensional models and computational probing of structure-function relations in G protein-coupled receptors
  publication-title: Methods Neurosci.
  doi: 10.1016/S1043-9471(05)80049-7
– volume: 48
  start-page: 479
  year: 2015
  end-page: 487
  ident: CR30
  article-title: Accelerated molecular dynamics simulations of ligand binding to a muscarinic G-protein-coupled receptor
  publication-title: Q. Rev. Biophys.
  doi: 10.1017/S0033583515000153
– volume: 64
  start-page: 112
  year: 2008
  end-page: 122
  ident: CR55
  article-title: A short history of SHELX
  publication-title: Acta Crystallogr. A.
  doi: 10.1107/S0108767307043930
– volume: 371
  start-page: 443
  year: 2003
  end-page: 449
  ident: CR36
  article-title: Identification by site-directed mutagenesis of amino acids contributing to ligand-binding specificity or signal transduction properties of the human FP prostanoid receptor
  publication-title: Biochem. J.
  doi: 10.1042/bj20021429
– volume: 494
  start-page: 185
  year: 2013
  end-page: 194
  ident: CR24
  article-title: Molecular signatures of G-protein-coupled receptors
  publication-title: Nature
  doi: 10.1038/nature11896
– volume: 25
  start-page: 2268
  year: 2016
  end-page: 2276
  ident: CR46
  article-title: The intervening removable affinity tag (iRAT) production system facilitates Fv antibody fragment-mediated crystallography
  publication-title: Protein Sci.
  doi: 10.1002/pro.3035
– volume: 1741
  start-page: 050021
  year: 2016
  ident: CR48
  article-title: Remote access and automation of SPring-8 MX beamlines
  publication-title: AIP Conf. Proc.
  doi: 10.1063/1.4952941
– volume: 12
  start-page: 281
  year: 2016
  end-page: 296
  ident: CR60
  article-title: OPLS3: a force field providing broad coverage of drug-like small molecules and proteins
  publication-title: J. Chem. Theory. Comput.
  doi: 10.1021/acs.jctc.5b00864
– volume: 357
  start-page: 73
  year: 1998
  end-page: 82
  ident: CR15
  article-title: A conserved threonine in the second extracellular loop of the human EP2 and EP4 receptors is required for ligand binding
  publication-title: Eur. J. Pharmacol.
  doi: 10.1016/S0014-2999(98)00522-6
– volume: 69
  start-page: 5
  year: 2006
  end-page: 10
  ident: CR2
  article-title: EP(4) prostanoid receptor coupling to a pertussis toxin-sensitive inhibitory G protein
  publication-title: Mol. Pharmacol.
– volume: 103
  start-page: 1492
  year: 2006
  end-page: 1497
  ident: CR3
  article-title: Role of beta-arrestin 1 in the metastatic progression of colorectal cancer
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0510562103
– volume: 754
  start-page: 179
  year: 2015
  end-page: 189
  ident: CR11
  article-title: KAG-308, a newly-identified EP4-selective agonist shows efficacy for treating ulcerative colitis and can bring about lower risk of colorectal carcinogenesis by oral administration
  publication-title: Eur. J. Pharmacol.
  doi: 10.1016/j.ejphar.2015.02.021
– volume: 3
  start-page: 350
  year: 2015
  ident: CR13
  article-title: Combination of EP4 antagonist and checkpoint inhibitors promotes anti-tumor effector T cells in preclinical tumor models
  publication-title: J. Immunother. Cancer
  doi: 10.1186/2051-1426-3-S2-P350
– volume: 66
  start-page: 486
  year: 2010
  end-page: 501
  ident: CR53
  article-title: Features and development of Coot
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444910007493
– volume: 9
  start-page: 1021
  year: 2012
  end-page: 1029
  ident: CR45
  article-title: TGFα shedding assay: an accurate and versatile method for detecting GPCR activation
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.2172
– volume: 111
  start-page: 6209
  year: 2011
  end-page: 6230
  ident: CR1
  article-title: Prostanoid receptors
  publication-title: Chem. Rev.
  doi: 10.1021/cr200010h
– volume: 15
  start-page: 633
  year: 2009
  end-page: 640
  ident: CR5
  article-title: Prostaglandin E2-EP4 signaling promotes immune inflammation through Th1 cell differentiation and Th17 cell expansion
  publication-title: Nat. Med.
  doi: 10.1038/nm.1968
– volume: 49
  start-page: 534
  year: 2006
  end-page: 553
  ident: CR59
  article-title: Novel procedure for modeling ligand/receptor induced fit effects
  publication-title: J. Med. Chem.
  doi: 10.1021/jm050540c
– volume: 6
  year: 2016
  ident: CR31
  article-title: The pathway of ligand entry from the membrane bilayer to a lipid G protein-coupled receptor
  publication-title: Sci. Rep.
  doi: 10.1038/srep22639
– volume: 44
  start-page: 934
  year: 1993
  end-page: 939
  ident: CR37
  article-title: Point mutation in the seventh hydrophobic domain of the human thromboxane A2 receptor allows discrimination between agonist and antagonist binding sites
  publication-title: Mol. Pharmacol.
– volume: 109
  start-page: 883
  year: 2002
  end-page: 893
  ident: CR23
  article-title: The prostaglandin receptor EP4 suppresses colitis, mucosal damage and CD4 cell activation in the gut
  publication-title: J. Clin. Invest.
  doi: 10.1172/JCI0214459
– volume: 545
  start-page: 112
  year: 2017
  end-page: 115
  ident: CR42
  article-title: Structural insight into allosteric modulation of protease-activated receptor 2
  publication-title: Nature
  doi: 10.1038/nature22309
– volume: 40
  start-page: 658
  year: 2007
  end-page: 674
  ident: CR52
  article-title: Phaser crystallographic software
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
– volume: 43
  start-page: 1215
  year: 2011
  end-page: 1218
  ident: CR7
  article-title: A genome-wide association study identifies new susceptibility loci for non-cardia gastric cancer at 3q13.31 and 5p13.1
  publication-title: Nat. Genet.
  doi: 10.1038/ng.978
– volume: 66
  start-page: 486
  year: 2010
  ident: 131_CR53
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444910007493
– volume: 9
  start-page: 1021
  year: 2012
  ident: 131_CR45
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.2172
– volume: 545
  start-page: 112
  year: 2017
  ident: 131_CR42
  publication-title: Nature
  doi: 10.1038/nature22309
– volume: 371
  start-page: 443
  year: 2003
  ident: 131_CR36
  publication-title: Biochem. J.
  doi: 10.1042/bj20021429
– volume: 64
  start-page: 112
  year: 2008
  ident: 131_CR55
  publication-title: Acta Crystallogr. A.
  doi: 10.1107/S0108767307043930
– volume: 48
  start-page: 479
  year: 2015
  ident: 131_CR30
  publication-title: Q. Rev. Biophys.
  doi: 10.1017/S0033583515000153
– volume: 11
  start-page: 78
  year: 2012
  ident: 131_CR17
  publication-title: Microb. Cell. Fact.
  doi: 10.1186/1475-2859-11-78
– volume: 69
  start-page: 1617
  year: 2013
  ident: 131_CR51
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444913012274
– ident: 131_CR22
– volume-title: AMBER 11
  year: 2010
  ident: 131_CR61
– volume: 278
  start-page: 4250
  year: 2003
  ident: 131_CR35
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M207420200
– volume: 49
  start-page: 377
  year: 2009
  ident: 131_CR58
  publication-title: J. Chem. Inf. Model.
  doi: 10.1021/ci800324m
– volume: 272
  start-page: 15154
  year: 1997
  ident: 131_CR14
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.272.24.15154
– volume: 79
  start-page: 1193
  year: 1999
  ident: 131_CR16
  publication-title: Physiol. Rev.
  doi: 10.1152/physrev.1999.79.4.1193
– volume: 25
  start-page: 366
  year: 1995
  ident: 131_CR20
  publication-title: Methods Neurosci.
  doi: 10.1016/S1043-9471(05)80049-7
– volume: 111
  start-page: 6209
  year: 2011
  ident: 131_CR1
  publication-title: Chem. Rev.
  doi: 10.1021/cr200010h
– volume: 546
  start-page: 259
  year: 2017
  ident: 131_CR43
  publication-title: Nature
  doi: 10.1038/nature22363
– volume: 22
  start-page: 57
  year: 2017
  ident: 131_CR9
  publication-title: Drug Discov. Today
  doi: 10.1016/j.drudis.2016.08.003
– volume: 44
  start-page: 934
  year: 1993
  ident: 131_CR37
  publication-title: Mol. Pharmacol.
– volume: 103
  start-page: 1492
  year: 2006
  ident: 131_CR3
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0510562103
– volume: 3
  start-page: 350
  year: 2015
  ident: 131_CR13
  publication-title: J. Immunother. Cancer
  doi: 10.1186/2051-1426-3-S2-P350
– volume: 69
  start-page: 5
  year: 2006
  ident: 131_CR2
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.105.017749
– volume: 45
  start-page: 907
  year: 2013
  ident: 131_CR8
  publication-title: Nat. Genet.
  doi: 10.1038/ng.2686
– volume: 40
  start-page: 658
  year: 2007
  ident: 131_CR52
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
– volume: 37
  start-page: 37
  year: 2016
  ident: 131_CR18
  publication-title: Trends Pharmacol. Sci.
  doi: 10.1016/j.tips.2015.09.005
– volume: 4
  start-page: 706
  year: 2009
  ident: 131_CR47
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2009.31
– volume: 161
  start-page: 1633
  year: 2015
  ident: 131_CR26
  publication-title: Cell
  doi: 10.1016/j.cell.2015.06.002
– volume: 51
  start-page: 61
  year: 1997
  ident: 131_CR34
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.51.1.61
– volume: 49
  start-page: 534
  year: 2006
  ident: 131_CR59
  publication-title: J. Med. Chem.
  doi: 10.1021/jm050540c
– volume: 66
  start-page: 125
  year: 2010
  ident: 131_CR50
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444909047337
– volume: 66
  start-page: 213
  year: 2010
  ident: 131_CR54
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444909052925
– volume: 16
  start-page: 787
  year: 2017
  ident: 131_CR41
  publication-title: Nat. Rev. Drug. Discov.
  doi: 10.1038/nrd.2017.91
– volume: 65
  start-page: 1010
  year: 2013
  ident: 131_CR4
  publication-title: Pharmacol. Rev.
  doi: 10.1124/pr.112.007195
– volume: 513
  start-page: 124
  year: 2014
  ident: 131_CR28
  publication-title: Nature
  doi: 10.1038/nature13494
– volume: 39
  start-page: 233
  year: 2014
  ident: 131_CR21
  publication-title: Trends. Biochem. Sci.
  doi: 10.1016/j.tibs.2014.03.002
– volume: 109
  start-page: 883
  year: 2002
  ident: 131_CR23
  publication-title: J. Clin. Invest.
  doi: 10.1172/JCI0214459
– volume: 289
  start-page: 739
  year: 2000
  ident: 131_CR29
  publication-title: Science
  doi: 10.1126/science.289.5480.739
– volume: 357
  start-page: 73
  year: 1998
  ident: 131_CR15
  publication-title: Eur. J. Pharmacol.
  doi: 10.1016/S0014-2999(98)00522-6
– volume: 25
  start-page: 2268
  year: 2016
  ident: 131_CR46
  publication-title: Protein Sci.
  doi: 10.1002/pro.3035
– volume: 74
  start-page: 441
  year: 2018
  ident: 131_CR49
  publication-title: Acta Crystallogr. D Struct. Biol.
  doi: 10.1107/S2059798318004576
– volume: 54
  start-page: 584
  year: 1998
  ident: 131_CR33
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.54.3.584
– volume: 83
  start-page: 206
  year: 2013
  ident: 131_CR38
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.112.080473
– volume: 331
  start-page: 297
  year: 2009
  ident: 131_CR44
  publication-title: J. Pharmacol. Exp. Ther.
  doi: 10.1124/jpet.109.156398
– volume: 121
  start-page: 6341
  year: 2017
  ident: 131_CR19
  publication-title: J. Phys. Chem. B
  doi: 10.1021/acs.jpcb.7b02997
– volume: 44
  start-page: 1285
  year: 2011
  ident: 131_CR56
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889811041768
– volume: 15
  start-page: 633
  year: 2009
  ident: 131_CR5
  publication-title: Nat. Med.
  doi: 10.1038/nm.1968
– volume: 62
  start-page: 28
  year: 2002
  ident: 131_CR32
  publication-title: Cancer Res.
– volume: 57
  start-page: 39
  year: 2012
  ident: 131_CR39
  publication-title: Rev. Roum. Chim.
– volume: 335
  start-page: 851
  year: 2012
  ident: 131_CR25
  publication-title: Science
  doi: 10.1126/science.1215904
– volume: 494
  start-page: 185
  year: 2013
  ident: 131_CR24
  publication-title: Nature
  doi: 10.1038/nature11896
– volume: 79
  start-page: 793
  year: 2011
  ident: 131_CR40
  publication-title: Sci. Pharm.
  doi: 10.3797/scipharm.1106-24
– volume: 754
  start-page: 179
  year: 2015
  ident: 131_CR11
  publication-title: Eur. J. Pharmacol.
  doi: 10.1016/j.ejphar.2015.02.021
– volume: 6
  year: 2016
  ident: 131_CR31
  publication-title: Sci. Rep.
  doi: 10.1038/srep22639
– volume: 3
  start-page: e58
  year: 2007
  ident: 131_CR6
  publication-title: PLoS. Genet.
  doi: 10.1371/journal.pgen.0030058
– volume: 43
  start-page: 1215
  year: 2011
  ident: 131_CR7
  publication-title: Nat. Genet.
  doi: 10.1038/ng.978
– volume: 30
  start-page: 756
  year: 2016
  ident: 131_CR12
  publication-title: J. Vet. Intern. Med.
  doi: 10.1111/jvim.13948
– volume: 372
  start-page: 774
  year: 2007
  ident: 131_CR57
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2007.05.022
– volume: 540
  start-page: 602
  year: 2016
  ident: 131_CR27
  publication-title: Nature
  doi: 10.1038/nature20613
– volume: 12
  start-page: 281
  year: 2016
  ident: 131_CR60
  publication-title: J. Chem. Theory. Comput.
  doi: 10.1021/acs.jctc.5b00864
– volume: 1741
  start-page: 050021
  year: 2016
  ident: 131_CR48
  publication-title: AIP Conf. Proc.
  doi: 10.1063/1.4952941
– volume: 38
  start-page: 1109
  year: 2016
  ident: 131_CR10
  publication-title: Clin. Ther.
  doi: 10.1016/j.clinthera.2016.02.019
SSID ssj0036618
Score 2.558815
Snippet Prostaglandin E receptor EP4, a G-protein-coupled receptor, is involved in disorders such as cancer and autoimmune disease. Here, we report the crystal...
SourceID proquest
crossref
springer
SourceType Aggregation Database
Enrichment Source
Index Database
Publisher
StartPage 18
SubjectTerms 631/154/436
631/45/535
631/45/535/1266
631/92/287
Allosteric properties
Binding
Biochemical Engineering
Biochemistry
Bioorganic Chemistry
Cancer
Cell Biology
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Crystal structure
Docking
Drug delivery
Drug development
G protein-coupled receptors
Ligands
Lipid bilayers
Lipids
Prostaglandin E
Prostaglandin E2
Proteins
Title Ligand binding to human prostaglandin E receptor EP4 at the lipid-bilayer interface
URI https://link.springer.com/article/10.1038/s41589-018-0131-3
https://www.proquest.com/docview/2154246869
https://www.proquest.com/docview/2149854489
Volume 15
WOSCitedRecordID wos000452634100011&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVPQU
  databaseName: Earth, Atmospheric & Aquatic Science Database
  customDbUrl:
  eissn: 1552-4469
  dateEnd: 20211231
  omitProxy: false
  ssIdentifier: ssj0036618
  issn: 1552-4450
  databaseCode: PCBAR
  dateStart: 20190101
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/eaasdb
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Materials Science Database
  customDbUrl:
  eissn: 1552-4469
  dateEnd: 20211231
  omitProxy: false
  ssIdentifier: ssj0036618
  issn: 1552-4450
  databaseCode: KB.
  dateStart: 20190101
  isFulltext: true
  titleUrlDefault: http://search.proquest.com/materialsscijournals
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Biological Science Database (NC LIVE)
  customDbUrl:
  eissn: 1552-4469
  dateEnd: 20211231
  omitProxy: false
  ssIdentifier: ssj0036618
  issn: 1552-4450
  databaseCode: M7P
  dateStart: 20190101
  isFulltext: true
  titleUrlDefault: http://search.proquest.com/biologicalscijournals
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Central
  customDbUrl:
  eissn: 1552-4469
  dateEnd: 20211231
  omitProxy: false
  ssIdentifier: ssj0036618
  issn: 1552-4450
  databaseCode: BENPR
  dateStart: 20190101
  isFulltext: true
  titleUrlDefault: https://www.proquest.com/central
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Health & Medical Collection (NC LIVE)
  customDbUrl:
  eissn: 1552-4469
  dateEnd: 20211231
  omitProxy: false
  ssIdentifier: ssj0036618
  issn: 1552-4450
  databaseCode: 7X7
  dateStart: 20190101
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/healthcomplete
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Science Database (NC LIVE)
  customDbUrl:
  eissn: 1552-4469
  dateEnd: 20211231
  omitProxy: false
  ssIdentifier: ssj0036618
  issn: 1552-4450
  databaseCode: M2P
  dateStart: 20190101
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/sciencejournals
  providerName: ProQuest
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1bi9QwFD64u4K-eNlVHF2HCOKDErdtkmnyJLvLLII6FC8wbyW3LoWx053pLvjvPcm0Myi4L76klKZNyUly7ucDeM0ES5wVjnKvOEX9S1HFrKHOZBKlk1y4pIpgE_lsJudzVfQGt3UfVjmcifGgdksbbOQnyJp4xidyoj60VzSgRgXvag-hsQcHoUpCgG74dPZ-OIkZ8p6YCidERjkXW68mkydrZFwhWCgNoVwspexPvrQTNv_yj0a2c_Hwf3_4ETzoBU5yulkhj-GObw7h6LRBZfvnL_KGxBDQaFs_hHvnA_zbEXz7XF_qxhFTx7wX0i1JxPMjbcgT0RH6o27IlOCR6VvU3Mm04ER3BCVKsqjb2qHSvdAo0ZNQkmJVaeufwI-L6ffzj7RHYKCWcdHRTFiRVamrpHcyq1DacInlHG8Ms9qEJDmR60RrVim8phY3uDLCJMz41AnDnsJ-s2z8MyCSWzdxFonkBHeKa24nuXXS5zYJFXZGkAzzX9q-PHlAyViU0U3OZLkhWYkkKwPJSjaCt9tX2k1tjts6Hw9kKvttui53NBrBq-1jnOjgNdGNX16HPlxJgVos9nk3LIbdJ_454PPbB3wB91H2UhtrzjHsd6tr_xLu2puuXq_GsJfP89jKMRycTWfF13Fc29h-yYrQ5sVvEVX8HA
linkProvider ProQuest
linkToHtml http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9QwEB6VglQuPFoQCwWMBBxAVpPY3sQHhKqyVasuq0oUaW_Br6BI2yTdTUH9U_xGxs5mVyDRWw-coiiOo9ifPTOexwfwmgkWWSMs5U5yivaXpJIZTa1OMtROUmGjIpBNpJNJNp3K0w341efC-LDKfk8MG7WtjT8j30PRxBM-zIbyY3NBPWuU9672FBodLE7c1U802RYfjj_h_L5JksPR2cERXbIKUMO4aGkijEiK2BaZs1lSoAS1keEcbzQzSvvEL5GqSClWSLzGBkErtdAR0y62QjPs9xbcxn089SFk6XRl4DGUdSH1ToiEYi8rLyrL9hYoKH1wUuxDx1hM2Z9ycK3c_uWPDWLu8P7_NkAP4N5SoSb73Qp4CBuu2oad_Uq19fkVeUtCiGvwHWzD1kFPb7cDX8bld1VZosuQ10PamgS-QtL4PBgVqE3KiowIigTXtPWcjE45US1BjZnMyqa0VJczhRYL8SU35oUy7hF8vZFffQybVV25J0AybuzQGtSvreBWcsXNMDU2c6mJfAWhAUT9fOdmWX7ds4DM8hAGwLK8g0iOEMk9RHI2gHerV5qu9sh1jXd7WOTLbWiRrzExgFerxzjQ3iukKldf-jZcZgKtdGzzvgffuot_fvDp9R98CVtHZ5_H-fh4cvIM7qKeKbuTq13YbOeX7jncMT_acjF_EdYQgW83jcnfqNpU5Q
linkToPdf http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1bb9MwFD4aHQJeuGwgCgOMBDyArCaxnTgPCJWuFdOmquIi7S1zbAdFKkloM9D-Gr-O41xagcTe9sBTFMVxFPuzv3N8bgAvmGCe0cJQbmNOUf-Kacx0Sk0aSJROImG8rCk2Ec3n8vQ0XuzArz4WxrlV9ntis1GbUrsz8hFSEw94KMN4lHVuEYvD2bvqO3UVpJyltS-n0ULk2F78RPVt_fboEOf6ZRDMpp8nH2hXYYBqxkVNA6FFkPkmk9bIIEM2NZ7mHG9SplXqgsBEpDylWBbj1dcI4DgVqcdS6xuRMuz3GuzKENfNAHYXk_fjjz0PMGS-JhBPiIBiPxubKpOjNdKmc1XynSMZ8yn7kxW3ou5f1tmG9GZ3_ufhugu3O1GbjNu1cQ92bLEH--NC1eW3C_KKNM6vjVVhD25O-sJ3-_DpJP-qCkPSvIn4IXVJmkqGpHIRMqopepIXZEqQLGxVlysyXXCiaoKyNFnmVW5omi8V6jLEJeNYZUrb-_DlSn71AQyKsrAPgUiuTWg0St5GcBNzxXUYaSNtpD2XW2gIXj_3ie4Ss7v6IMukcRBgMmnhkiBcEgeXhA3h9eaVqs1Kclnjgx4iSbdBrZMtPobwfPMYB9rZi1Rhy3PXhsdSoP6Obd70QNx28c8PPrr8g8_gBkIxOTmaHz-GWyiAxu2R1gEM6tW5fQLX9Y86X6-edguKwNlVg_I32nNe5Q
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Ligand+binding+to+human+prostaglandin+E+receptor+EP4+at+the+lipid-bilayer+interface&rft.jtitle=Nature+chemical+biology&rft.au=Toyoda%2C+Yosuke&rft.au=Morimoto%2C+Kazushi&rft.au=Suno%2C+Ryoji&rft.au=Horita%2C+Shoichiro&rft.date=2019-01-01&rft.pub=Nature+Publishing+Group+US&rft.issn=1552-4450&rft.eissn=1552-4469&rft.volume=15&rft.issue=1&rft.spage=18&rft.epage=26&rft_id=info:doi/10.1038%2Fs41589-018-0131-3&rft.externalDocID=10_1038_s41589_018_0131_3
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1552-4450&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1552-4450&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1552-4450&client=summon