Structure and activation of the TSH receptor transmembrane domain
Purpose The thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves’ disease. The TSHR is composed of: a leucine-rich repeat domain (LRD), a hinge region or cleavage domain (CD) and a transmembrane domain (TMD). The binding arrangements bet...
Uloženo v:
| Vydáno v: | Autoimmunity highlights Ročník 8; číslo 1; s. 2 |
|---|---|
| Hlavní autoři: | , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
Cham
Springer International Publishing
01.12.2017
Springer Nature B.V |
| Témata: | |
| ISSN: | 2038-0305, 2038-3274 |
| On-line přístup: | Získat plný text |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|
| Abstract | Purpose
The thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves’ disease. The TSHR is composed of: a leucine-rich repeat domain (LRD), a hinge region or cleavage domain (CD) and a transmembrane domain (TMD). The binding arrangements between the TSHR LRD and the thyroid-stimulating autoantibody M22 or TSH have become available from the crystal structure of the TSHR LRD–M22 complex and a comparative model of the TSHR LRD in complex with TSH, respectively. However, the mechanism by which the TMD of the TSHR and the other glycoprotein hormone receptors (GPHRs) becomes activated is unknown.
Methods
We have generated comparative models of the structures of the inactive (TMD_In) and active (TMD_Ac) conformations of the TSHR, follicle-stimulating hormone receptor (FSHR) and luteinizing hormone receptor (LHR) TMDs. The structures of TMD_Ac and TMD_In were obtained using class A GPCR crystal structures for which fully active and inactive conformations were available.
Results
Most conserved motifs observed in GPCR TMDs are also observed in the amino acid sequences of GPHR TMDs. Furthermore, most GPCR TMD conserved helix distortions are observed in our models of the structures of GPHR TMDs. Analysis of these structures has allowed us to propose a mechanism for activation of GPHR TMDs.
Conclusions
Insight into the mechanism of activation of the TSHR by both TSH and TSHR autoantibodies is likely to be useful in the development of new treatments for Graves’ disease. |
|---|---|
| AbstractList | PurposeThe thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves’ disease. The TSHR is composed of: a leucine-rich repeat domain (LRD), a hinge region or cleavage domain (CD) and a transmembrane domain (TMD). The binding arrangements between the TSHR LRD and the thyroid-stimulating autoantibody M22 or TSH have become available from the crystal structure of the TSHR LRD–M22 complex and a comparative model of the TSHR LRD in complex with TSH, respectively. However, the mechanism by which the TMD of the TSHR and the other glycoprotein hormone receptors (GPHRs) becomes activated is unknown.MethodsWe have generated comparative models of the structures of the inactive (TMD_In) and active (TMD_Ac) conformations of the TSHR, follicle-stimulating hormone receptor (FSHR) and luteinizing hormone receptor (LHR) TMDs. The structures of TMD_Ac and TMD_In were obtained using class A GPCR crystal structures for which fully active and inactive conformations were available.ResultsMost conserved motifs observed in GPCR TMDs are also observed in the amino acid sequences of GPHR TMDs. Furthermore, most GPCR TMD conserved helix distortions are observed in our models of the structures of GPHR TMDs. Analysis of these structures has allowed us to propose a mechanism for activation of GPHR TMDs.ConclusionsInsight into the mechanism of activation of the TSHR by both TSH and TSHR autoantibodies is likely to be useful in the development of new treatments for Graves’ disease. Purpose The thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves’ disease. The TSHR is composed of: a leucine-rich repeat domain (LRD), a hinge region or cleavage domain (CD) and a transmembrane domain (TMD). The binding arrangements between the TSHR LRD and the thyroid-stimulating autoantibody M22 or TSH have become available from the crystal structure of the TSHR LRD–M22 complex and a comparative model of the TSHR LRD in complex with TSH, respectively. However, the mechanism by which the TMD of the TSHR and the other glycoprotein hormone receptors (GPHRs) becomes activated is unknown. Methods We have generated comparative models of the structures of the inactive (TMD_In) and active (TMD_Ac) conformations of the TSHR, follicle-stimulating hormone receptor (FSHR) and luteinizing hormone receptor (LHR) TMDs. The structures of TMD_Ac and TMD_In were obtained using class A GPCR crystal structures for which fully active and inactive conformations were available. Results Most conserved motifs observed in GPCR TMDs are also observed in the amino acid sequences of GPHR TMDs. Furthermore, most GPCR TMD conserved helix distortions are observed in our models of the structures of GPHR TMDs. Analysis of these structures has allowed us to propose a mechanism for activation of GPHR TMDs. Conclusions Insight into the mechanism of activation of the TSHR by both TSH and TSHR autoantibodies is likely to be useful in the development of new treatments for Graves’ disease. The thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves' disease. The TSHR is composed of: a leucine-rich repeat domain (LRD), a hinge region or cleavage domain (CD) and a transmembrane domain (TMD). The binding arrangements between the TSHR LRD and the thyroid-stimulating autoantibody M22 or TSH have become available from the crystal structure of the TSHR LRD-M22 complex and a comparative model of the TSHR LRD in complex with TSH, respectively. However, the mechanism by which the TMD of the TSHR and the other glycoprotein hormone receptors (GPHRs) becomes activated is unknown. We have generated comparative models of the structures of the inactive (TMD_In) and active (TMD_Ac) conformations of the TSHR, follicle-stimulating hormone receptor (FSHR) and luteinizing hormone receptor (LHR) TMDs. The structures of TMD_Ac and TMD_In were obtained using class A GPCR crystal structures for which fully active and inactive conformations were available. Most conserved motifs observed in GPCR TMDs are also observed in the amino acid sequences of GPHR TMDs. Furthermore, most GPCR TMD conserved helix distortions are observed in our models of the structures of GPHR TMDs. Analysis of these structures has allowed us to propose a mechanism for activation of GPHR TMDs. Insight into the mechanism of activation of the TSHR by both TSH and TSHR autoantibodies is likely to be useful in the development of new treatments for Graves' disease. |
| ArticleNumber | 2 |
| Author | Furmaniak, Jadwiga Smith, Bernard Rees Núñez Miguel, Ricardo Sanders, Jane |
| Author_xml | – sequence: 1 givenname: Ricardo surname: Núñez Miguel fullname: Núñez Miguel, Ricardo organization: FIRS Laboratories, RSR Ltd – sequence: 2 givenname: Jane surname: Sanders fullname: Sanders, Jane organization: FIRS Laboratories, RSR Ltd – sequence: 3 givenname: Jadwiga surname: Furmaniak fullname: Furmaniak, Jadwiga organization: FIRS Laboratories, RSR Ltd – sequence: 4 givenname: Bernard Rees surname: Smith fullname: Smith, Bernard Rees email: firs@rsrltd.eclipse.co.uk organization: FIRS Laboratories, RSR Ltd |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27921237$$D View this record in MEDLINE/PubMed |
| BookMark | eNp9UUFPHCEYJWaNu7X-AC9mkl68TOWDYZi5NNkYW5uYeFDPBBhQzAxsgTHpvy92t9qaVC4fyffe4z3eB7TwwRuEjgF_Boz5WQJKgdcY2hrjHtewh1YE066mhDeL3R1TzJboKKVHXA7tywofoCXhPQFC-Qqtb3KcdZ6jqaQfKqmze5LZBV8FW-UHU93eXFbRaLPJIVY5Sp8mM6kyTTWESTr_Ee1bOSZztJuH6O7rxe35ZX11_e37-fqq1g3HuSa0ZVRqbi1oYntsGWtaxdTAZSeJJaCsZQ2AIkrKfuh6iRXXoLjUPSWS0EP0Zau7mdVkBm18cTOKTXSTjD9FkE78u_HuQdyHJ8GAti3risDpTiCGH7NJWUwuaTOOJUuYk4CuaWnbEdoU6Kc30McwR1_iCdIQTjl0jBbUyd-OXqz8-d0CgC1Ax5BSNPYFAlg8lyi2JYpSonguUUDh8Dcc7fLvRkooN77LJFtmKq_4exNfTf-f9AuDgq_g |
| CitedBy_id | crossref_primary_10_3389_fendo_2017_00086 crossref_primary_10_1210_endocr_bqad146 crossref_primary_10_1016_j_emc_2023_06_005 crossref_primary_10_1134_S0022093022050143 crossref_primary_10_1002_pmic_201800307 crossref_primary_10_1080_10495398_2021_1992415 crossref_primary_10_1210_endocr_bqab051 crossref_primary_10_1210_js_2018_00077 crossref_primary_10_3390_molecules25092185 crossref_primary_10_1007_s40618_021_01663_9 crossref_primary_10_1016_j_jmb_2018_10_005 crossref_primary_10_1038_s41422_022_00751_6 crossref_primary_10_23736_S1824_4785_21_03344_6 crossref_primary_10_1002_jcla_23950 crossref_primary_10_1134_S1607672920020064 crossref_primary_10_1186_s13317_019_0125_5 |
| Cites_doi | 10.1126/science.289.5480.739 10.1038/nature12572 10.1530/REP-13-0351 10.1530/eje.0.1430471 10.1038/nature12167 10.1210/mend.14.8.0510 10.1016/j.ijbiomac.2015.12.072 10.1210/edrv-9-1-106 10.1210/edrv.21.5.0409 10.1210/jcem.87.6.8523 10.1080/07391102.2014.932310 10.1016/j.tips.2011.09.003 10.1007/s001090000170 10.1038/nature03206 10.1172/JCI3795 10.1038/nature07101 10.1126/science.1164772 10.3390/ijms15057841 10.1210/jc.2015-1401 10.1006/clin.1997.4412 10.1210/jcem.87.3.8319 10.1111/j.1365-2265.2008.03333.x 10.1002/prot.24195 10.1073/pnas.1206643109 10.1210/en.2014-1509 10.1006/jmbi.1993.1626 10.1530/rep.1.00663 10.1038/491021a 10.1074/jbc.M102244200 10.1038/nature10753 10.1210/mend.13.11.0370 10.1016/S0076-6879(03)74020-8 10.1074/jbc.M110.196980 10.1038/nature10939 10.1089/thy.2004.14.991 10.1074/jbc.M703500200 10.1186/1756-6614-4-S1-S8 10.1093/nar/22.22.4673 10.1371/journal.pone.0142250 10.1371/journal.pone.0138463 10.1126/science.1215904 10.1038/nature09789 10.1126/science.1150577 10.1096/fj.09-149146 10.1038/nature11701 10.1038/nature10954 10.1111/j.1365-2265.2010.03872.x 10.1210/jcem.83.2.4579 10.1038/nature11085 10.1089/thy.2007.0034 10.1038/nature06925 10.1007/s00018-010-0451-2 10.1038/365652a0 10.1507/endocrj.K06-090 10.1074/jbc.M203272200 10.1074/jbc.M406948200 10.1074/jbc.M414678200 10.1210/mend.14.8.0503 10.1210/mend.12.6.0124 10.1210/jc.2014-1436 10.1038/nature10361 10.1021/bi050938a 10.1006/mgme.1998.2780 10.1210/jc.2011-2106 10.1038/nature10236 10.1074/jbc.M115.709659 10.1210/mend.15.8.0672 10.1038/nature12735 10.1016/j.jmb.2004.07.044 10.1038/nature11111 10.1016/S1043-9471(05)80049-7 10.1038/nature10867 10.1038/ng0295-160 10.1210/jc.2014-3662 10.1073/pnas.92.6.1906 10.1016/j.pharmthera.2014.02.004 10.1007/s00210-002-0588-0 10.1126/science.1194396 |
| ContentType | Journal Article |
| Copyright | The Author(s) 2016 The Author(s) 2016. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
| Copyright_xml | – notice: The Author(s) 2016 – notice: The Author(s) 2016. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
| DBID | C6C AAYXX CITATION NPM 8FE 8FH ABUWG AFKRA AZQEC BBNVY BENPR BHPHI CCPQU DWQXO GNUQQ HCIFZ LK8 M7P PHGZM PHGZT PIMPY PKEHL PQEST PQGLB PQQKQ PQUKI PRINS 7X8 5PM |
| DOI | 10.1007/s13317-016-0090-1 |
| DatabaseName | Springer Nature OA Free Journals CrossRef PubMed ProQuest SciTech Collection ProQuest Natural Science Journals ProQuest Central (Alumni) ProQuest Central UK/Ireland ProQuest Central Essentials Biological Science Collection ProQuest Central Natural Science Collection ProQuest One Community College ProQuest Central ProQuest Central Student SciTech Premium Collection Biological Sciences Biological Science Database ProQuest Central Premium ProQuest One Academic Publicly Available Content Database ProQuest One Academic Middle East (New) ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef PubMed Publicly Available Content Database ProQuest Central Student ProQuest One Academic Middle East (New) ProQuest Biological Science Collection ProQuest Central Essentials ProQuest One Academic Eastern Edition ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest Natural Science Collection Biological Science Database ProQuest SciTech Collection ProQuest Central China ProQuest Central ProQuest One Applied & Life Sciences ProQuest One Academic UKI Edition Natural Science Collection ProQuest Central Korea Biological Science Collection ProQuest Central (New) ProQuest One Academic ProQuest One Academic (New) MEDLINE - Academic |
| DatabaseTitleList | Publicly Available Content Database MEDLINE - Academic PubMed |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: PIMPY name: Publicly Available Content Database url: http://search.proquest.com/publiccontent sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 2038-3274 |
| EndPage | 2 |
| ExternalDocumentID | PMC5136658 27921237 10_1007_s13317_016_0090_1 |
| Genre | Journal Article |
| GroupedDBID | --- 06D 0R~ 0VY 2JY 30V 4.4 408 409 53G 67N 8TC ABBXA ABDBF ACGFS ACPRK ACUHS ADBBV ADRAZ ADUKV AFBBN AFKRA AFWTZ AHBYD AHYZX AKMHD ALMA_UNASSIGNED_HOLDINGS AMKLP AOIJS BAPOH BAWUL BBNVY BENPR BFQNJ BGNMA BHPHI BMC C6C CCPQU DIK EBLON EBS EJD G-Y G-Z GQ7 GQ8 H13 HCIFZ HMJXF HYE I0C IZIGR J0Z KOV KQ8 M48 M4Y M7P NU0 O93 O9I OK1 PGMZT PHGZM PHGZT PIMPY PQGLB PUEGO QOS R9I ROL RPM RSV S27 S3A S3B SBL SHX SOJ T13 U2A WK8 Z45 ~A9 2VQ 8FE 8FH AAIAL AAYXX ABFSG ACSTC AEZWR AFFHD AFHIU AHSBF AHWEU AIXLP CITATION HF~ HZ~ IAO ITC LK8 O9- S1Z AAYZH NPM ABUWG AZQEC DWQXO GNUQQ PKEHL PQEST PQQKQ PQUKI PRINS 7X8 5PM |
| ID | FETCH-LOGICAL-c470t-23653ac7ff1c2f90f5546b5bd7a8a2f21bff5411b2baa9d89a0b7c1b7ac932a23 |
| IEDL.DBID | M7P |
| ISICitedReferencesCount | 21 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000390887200002&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 2038-0305 |
| IngestDate | Tue Nov 04 01:49:28 EST 2025 Sun Nov 09 09:15:06 EST 2025 Fri Jul 25 11:11:53 EDT 2025 Thu Apr 03 06:49:58 EDT 2025 Sat Nov 29 02:51:50 EST 2025 Tue Nov 18 22:14:22 EST 2025 Sat Sep 06 07:28:21 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Keywords | TSHR structure Glycoprotein hormones Graves’ disease TSHR activation Transmembrane domain structure Glycoprotein hormone receptors |
| Language | English |
| License | Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c470t-23653ac7ff1c2f90f5546b5bd7a8a2f21bff5411b2baa9d89a0b7c1b7ac932a23 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| OpenAccessLink | https://www.proquest.com/docview/2427371853?pq-origsite=%requestingapplication% |
| PMID | 27921237 |
| PQID | 2427371853 |
| PQPubID | 2043794 |
| PageCount | 1 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_5136658 proquest_miscellaneous_1846368234 proquest_journals_2427371853 pubmed_primary_27921237 crossref_primary_10_1007_s13317_016_0090_1 crossref_citationtrail_10_1007_s13317_016_0090_1 springer_journals_10_1007_s13317_016_0090_1 |
| PublicationCentury | 2000 |
| PublicationDate | 2017-12-01 |
| PublicationDateYYYYMMDD | 2017-12-01 |
| PublicationDate_xml | – month: 12 year: 2017 text: 2017-12-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Cham |
| PublicationPlace_xml | – name: Cham – name: England – name: Heidelberg |
| PublicationTitle | Autoimmunity highlights |
| PublicationTitleAbbrev | Autoimmun Highlights |
| PublicationTitleAlternate | Auto Immun Highlights |
| PublicationYear | 2017 |
| Publisher | Springer International Publishing Springer Nature B.V |
| Publisher_xml | – name: Springer International Publishing – name: Springer Nature B.V |
| References | JW Martens (90_CR83) 2002; 87 A Manglik (90_CR60) 2012; 485 J Gromoll (90_CR67) 1998; 83 E Doherty (90_CR78) 2002; 87 H Kremer (90_CR71) 1999; 84 X Jiang (90_CR9) 2012; 109 E Nishihara (90_CR42) 2006; 53 V Chantreau (90_CR11) 2015; 10 S Kosugi (90_CR40) 2000; 143 E Urizar (90_CR16) 2005; 280 JD Thompson (90_CR26) 1994; 22 R Núñez Miguel (90_CR18) 2004; 14 AA Thompson (90_CR61) 2012; 485 SM Wu (90_CR49) 1999; 66 K Palczewski (90_CR3) 2000; 289 S Bhattacharya (90_CR4) 2013; 81 VP Jaakola (90_CR53) 2008; 322 R Seifert (90_CR34) 2002; 366 H Wu (90_CR59) 2012; 485 QR Fan (90_CR8) 2005; 433 S Granier (90_CR62) 2012; 485 S Katari (90_CR77) 2015; 100 AK Haas (90_CR86) 2011; 68 J Parma (90_CR45) 1997; 82 T Warne (90_CR51) 2008; 454 SY Hsu (90_CR5) 2000; 14 B Trülzsch (90_CR41) 2001; 78 MA Hanson (90_CR56) 2012; 335 J Schaarschmidt (90_CR10) 2016; 291 G Kleinau (90_CR73) 2010; 24 C Zhang (90_CR57) 2012; 492 AC Latronico (90_CR69) 1995; 80 A Porcellini (90_CR43) 1994; 79 B Rees Smith (90_CR1) 1988; 9 AL Martin (90_CR35) 2015; 10 M Murakami (90_CR52) 2008; 453 G Kleinau (90_CR15) 2011; 286 SG Rasmussen (90_CR20) 2011; 477 AC Latronico (90_CR46) 1998; 83 SS Desai (90_CR80) 2015; 100 P Touraine (90_CR81) 1999; 13 WR Moyle (90_CR17) 2004; 279 YX Tao (90_CR66) 2000; 14 V Cherezov (90_CR23) 2007; 318 R Kant van der (90_CR30) 2014; 15 AC Kruse (90_CR58) 2012; 482 C Govaerts (90_CR38) 2001; 276 JWM Martens (90_CR85) 1998; 12 T Okada (90_CR22) 2004; 342 JA Ballesteros (90_CR27) 1995; 25 J Sanders (90_CR6) 2007; 17 L Laue (90_CR48) 1995; 92 MR Ali (90_CR13) 2014; 33 R Kraaij (90_CR68) 1995; 80 J Sande Van (90_CR36) 1995; 80 BG Tehan (90_CR37) 2014; 143 H Jaeschke (90_CR75) 2010; 73 H Jaeschke (90_CR14) 2014; 99 APN Themmen (90_CR70) 2000; 21 K Angelova (90_CR72) 2002; 277 H Biebermann (90_CR74) 2011; 4 S Fiser (90_CR32) 2003; 374 M Zhang (90_CR64) 2007; 282 A Shenker (90_CR47) 1993; 365 SS Desai (90_CR65) 2013; 146 I Beau (90_CR79) 1998; 102 P Sanders (90_CR7) 2011; 46 AC Kruse (90_CR21) 2013; 504 D Russo (90_CR44) 1996; 81 G Marco De (90_CR87) 2009; 70 H Biebermann (90_CR76) 2012; 97 HW Choe (90_CR19) 2011; 471 R Latif (90_CR12) 2015; 156 FI Khan (90_CR33) 2016; 85 S Neumann (90_CR39) 2001; 15 APN Themmen (90_CR82) 2005; 130 C Wang (90_CR63) 2013; 497 K Haga (90_CR24) 2012; 482 AM Ring (90_CR31) 2013; 502 H Kremer (90_CR84) 1995; 9 A Sali (90_CR25) 1993; 234 V Katritch (90_CR28) 2012; 33 W Xu (90_CR29) 2005; 44 B Wu (90_CR54) 2010; 330 T Shimamura (90_CR55) 2011; 475 DL Jacobson (90_CR2) 1997; 84 SH Park (90_CR50) 2012; 491 |
| References_xml | – volume: 289 start-page: 739 year: 2000 ident: 90_CR3 publication-title: Science doi: 10.1126/science.289.5480.739 – volume: 80 start-page: 2577 year: 1995 ident: 90_CR36 publication-title: J Clin Endocrinol Metab – volume: 502 start-page: 575 year: 2013 ident: 90_CR31 publication-title: Nature doi: 10.1038/nature12572 – volume: 82 start-page: 2695 year: 1997 ident: 90_CR45 publication-title: J Clin Endocrinol Metab – volume: 146 start-page: R235 year: 2013 ident: 90_CR65 publication-title: Reproduction doi: 10.1530/REP-13-0351 – volume: 143 start-page: 471 year: 2000 ident: 90_CR40 publication-title: Eur J Endocrinol doi: 10.1530/eje.0.1430471 – volume: 497 start-page: 338 year: 2013 ident: 90_CR63 publication-title: Nature doi: 10.1038/nature12167 – volume: 14 start-page: 1257 year: 2000 ident: 90_CR5 publication-title: Mol Endocrinol doi: 10.1210/mend.14.8.0510 – volume: 85 start-page: 48 year: 2016 ident: 90_CR33 publication-title: Int J Biol Macromol doi: 10.1016/j.ijbiomac.2015.12.072 – volume: 9 start-page: 106 year: 1988 ident: 90_CR1 publication-title: Endocr Rev doi: 10.1210/edrv-9-1-106 – volume: 21 start-page: 551 year: 2000 ident: 90_CR70 publication-title: Endocr Rev doi: 10.1210/edrv.21.5.0409 – volume: 87 start-page: 2506 year: 2002 ident: 90_CR83 publication-title: J Clin Endocrinol Metab doi: 10.1210/jcem.87.6.8523 – volume: 33 start-page: 1140 year: 2014 ident: 90_CR13 publication-title: J Biomol Struct Dyn doi: 10.1080/07391102.2014.932310 – volume: 33 start-page: 17 year: 2012 ident: 90_CR28 publication-title: Trends Pharmacol Sci doi: 10.1016/j.tips.2011.09.003 – volume: 78 start-page: 684 year: 2001 ident: 90_CR41 publication-title: J Mol Med doi: 10.1007/s001090000170 – volume: 433 start-page: 269 year: 2005 ident: 90_CR8 publication-title: Nature doi: 10.1038/nature03206 – volume: 102 start-page: 1352 year: 1998 ident: 90_CR79 publication-title: J Clin Investig doi: 10.1172/JCI3795 – volume: 454 start-page: 486 year: 2008 ident: 90_CR51 publication-title: Nature doi: 10.1038/nature07101 – volume: 322 start-page: 1211 year: 2008 ident: 90_CR53 publication-title: Science doi: 10.1126/science.1164772 – volume: 80 start-page: 3168 year: 1995 ident: 90_CR68 publication-title: J Clin Endocrinol Metab – volume: 15 start-page: 7841 year: 2014 ident: 90_CR30 publication-title: Int J Mol Sci doi: 10.3390/ijms15057841 – volume: 100 start-page: 2154 year: 2015 ident: 90_CR77 publication-title: J Clin Endocrinol Metab doi: 10.1210/jc.2015-1401 – volume: 84 start-page: 223 year: 1997 ident: 90_CR2 publication-title: Clin Immunol Immunopathol doi: 10.1006/clin.1997.4412 – volume: 46 start-page: 81 year: 2011 ident: 90_CR7 publication-title: J Mol Endocrinol – volume: 87 start-page: 1151 year: 2002 ident: 90_CR78 publication-title: J Clin Endocrinol Metab doi: 10.1210/jcem.87.3.8319 – volume: 70 start-page: 335 year: 2009 ident: 90_CR87 publication-title: Clin Endocrinol doi: 10.1111/j.1365-2265.2008.03333.x – volume: 81 start-page: 729 year: 2013 ident: 90_CR4 publication-title: Proteins doi: 10.1002/prot.24195 – volume: 109 start-page: 12491 year: 2012 ident: 90_CR9 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.1206643109 – volume: 156 start-page: 488 year: 2015 ident: 90_CR12 publication-title: Endocrinology doi: 10.1210/en.2014-1509 – volume: 234 start-page: 779 year: 1993 ident: 90_CR25 publication-title: J Mol Biol doi: 10.1006/jmbi.1993.1626 – volume: 130 start-page: 263 year: 2005 ident: 90_CR82 publication-title: Reproduction doi: 10.1530/rep.1.00663 – volume: 491 start-page: 779 year: 2012 ident: 90_CR50 publication-title: Nature doi: 10.1038/491021a – volume: 276 start-page: 22991 year: 2001 ident: 90_CR38 publication-title: J Biol Chem doi: 10.1074/jbc.M102244200 – volume: 482 start-page: 547 year: 2012 ident: 90_CR24 publication-title: Nature doi: 10.1038/nature10753 – volume: 81 start-page: 1548 year: 1996 ident: 90_CR44 publication-title: J Clin Endocrinol Metab – volume: 79 start-page: 657 year: 1994 ident: 90_CR43 publication-title: J Clin Endocrinol Metab – volume: 13 start-page: 1844 year: 1999 ident: 90_CR81 publication-title: Mol Endocrinol doi: 10.1210/mend.13.11.0370 – volume: 374 start-page: 461 year: 2003 ident: 90_CR32 publication-title: Method Enzymol doi: 10.1016/S0076-6879(03)74020-8 – volume: 286 start-page: 25859 year: 2011 ident: 90_CR15 publication-title: J Biol Chem doi: 10.1074/jbc.M110.196980 – volume: 485 start-page: 327 year: 2012 ident: 90_CR59 publication-title: Nature doi: 10.1038/nature10939 – volume: 14 start-page: 991 year: 2004 ident: 90_CR18 publication-title: Thyroid doi: 10.1089/thy.2004.14.991 – volume: 282 start-page: 25527 year: 2007 ident: 90_CR64 publication-title: J Biol Chem doi: 10.1074/jbc.M703500200 – volume: 4 start-page: S8 issue: Suppl 1 year: 2011 ident: 90_CR74 publication-title: Thyroid Res doi: 10.1186/1756-6614-4-S1-S8 – volume: 22 start-page: 4673 year: 1994 ident: 90_CR26 publication-title: Nucleic Acids Res doi: 10.1093/nar/22.22.4673 – volume: 10 start-page: e0142250 year: 2015 ident: 90_CR11 publication-title: PLoS One doi: 10.1371/journal.pone.0142250 – volume: 10 start-page: e0138463 year: 2015 ident: 90_CR35 publication-title: PLoS One doi: 10.1371/journal.pone.0138463 – volume: 335 start-page: 851 year: 2012 ident: 90_CR56 publication-title: Science doi: 10.1126/science.1215904 – volume: 471 start-page: 651 year: 2011 ident: 90_CR19 publication-title: Nature doi: 10.1038/nature09789 – volume: 318 start-page: 1258 year: 2007 ident: 90_CR23 publication-title: Science doi: 10.1126/science.1150577 – volume: 83 start-page: 2435 year: 1998 ident: 90_CR46 publication-title: J Clin Endocrinol Metab – volume: 80 start-page: 2490 year: 1995 ident: 90_CR69 publication-title: J Clin Endocrinol Metab – volume: 24 start-page: 2347 year: 2010 ident: 90_CR73 publication-title: FASEB J doi: 10.1096/fj.09-149146 – volume: 492 start-page: 387 year: 2012 ident: 90_CR57 publication-title: Nature doi: 10.1038/nature11701 – volume: 485 start-page: 321 year: 2012 ident: 90_CR60 publication-title: Nature doi: 10.1038/nature10954 – volume: 73 start-page: 815 year: 2010 ident: 90_CR75 publication-title: Clin Endocrinol doi: 10.1111/j.1365-2265.2010.03872.x – volume: 84 start-page: 1136 year: 1999 ident: 90_CR71 publication-title: J Clin Endocrinol Metab – volume: 83 start-page: 476 year: 1998 ident: 90_CR67 publication-title: J Clin Endocrinol Metab doi: 10.1210/jcem.83.2.4579 – volume: 485 start-page: 395 year: 2012 ident: 90_CR61 publication-title: Nature doi: 10.1038/nature11085 – volume: 17 start-page: 395 year: 2007 ident: 90_CR6 publication-title: Thyroid doi: 10.1089/thy.2007.0034 – volume: 453 start-page: 363 year: 2008 ident: 90_CR52 publication-title: Nature doi: 10.1038/nature06925 – volume: 68 start-page: 159 year: 2011 ident: 90_CR86 publication-title: Cell Mol Life Sci doi: 10.1007/s00018-010-0451-2 – volume: 365 start-page: 652 year: 1993 ident: 90_CR47 publication-title: Nature doi: 10.1038/365652a0 – volume: 53 start-page: 735 year: 2006 ident: 90_CR42 publication-title: Endocr J doi: 10.1507/endocrj.K06-090 – volume: 277 start-page: 32202 year: 2002 ident: 90_CR72 publication-title: J Biol Chem doi: 10.1074/jbc.M203272200 – volume: 279 start-page: 44442 year: 2004 ident: 90_CR17 publication-title: J Biol Chem doi: 10.1074/jbc.M406948200 – volume: 280 start-page: 17135 year: 2005 ident: 90_CR16 publication-title: J Biol Chem doi: 10.1074/jbc.M414678200 – volume: 14 start-page: 1272 year: 2000 ident: 90_CR66 publication-title: Mol Endocrinol doi: 10.1210/mend.14.8.0503 – volume: 12 start-page: 775 year: 1998 ident: 90_CR85 publication-title: Mol Endocrinol doi: 10.1210/mend.12.6.0124 – volume: 99 start-page: E2051 year: 2014 ident: 90_CR14 publication-title: J Clin Endocrinol Metab doi: 10.1210/jc.2014-1436 – volume: 477 start-page: 549 year: 2011 ident: 90_CR20 publication-title: Nature doi: 10.1038/nature10361 – volume: 44 start-page: 16014 year: 2005 ident: 90_CR29 publication-title: Biochemistry doi: 10.1021/bi050938a – volume: 66 start-page: 68 year: 1999 ident: 90_CR49 publication-title: Mol Genet Metab doi: 10.1006/mgme.1998.2780 – volume: 97 start-page: E228 year: 2012 ident: 90_CR76 publication-title: J Clin Endocrinol Metab doi: 10.1210/jc.2011-2106 – volume: 475 start-page: 65 year: 2011 ident: 90_CR55 publication-title: Nature doi: 10.1038/nature10236 – volume: 291 start-page: 14095 year: 2016 ident: 90_CR10 publication-title: J Biol Chem doi: 10.1074/jbc.M115.709659 – volume: 15 start-page: 1294 year: 2001 ident: 90_CR39 publication-title: Mol Endocrinol doi: 10.1210/mend.15.8.0672 – volume: 504 start-page: 101 year: 2013 ident: 90_CR21 publication-title: Nature doi: 10.1038/nature12735 – volume: 342 start-page: 571 year: 2004 ident: 90_CR22 publication-title: J Mol Biol doi: 10.1016/j.jmb.2004.07.044 – volume: 485 start-page: 400 year: 2012 ident: 90_CR62 publication-title: Nature doi: 10.1038/nature11111 – volume: 25 start-page: 366 year: 1995 ident: 90_CR27 publication-title: Methods Neurosci doi: 10.1016/S1043-9471(05)80049-7 – volume: 482 start-page: 552 year: 2012 ident: 90_CR58 publication-title: Nature doi: 10.1038/nature10867 – volume: 9 start-page: 160 year: 1995 ident: 90_CR84 publication-title: Nat Genet doi: 10.1038/ng0295-160 – volume: 100 start-page: E638 year: 2015 ident: 90_CR80 publication-title: J Clin Endocrinol Metab doi: 10.1210/jc.2014-3662 – volume: 92 start-page: 1906 year: 1995 ident: 90_CR48 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.92.6.1906 – volume: 143 start-page: 51 year: 2014 ident: 90_CR37 publication-title: Pharmacol Therapeut doi: 10.1016/j.pharmthera.2014.02.004 – volume: 366 start-page: 381 year: 2002 ident: 90_CR34 publication-title: Naunyn-Schmiedeberg’s Arch Pharmacol doi: 10.1007/s00210-002-0588-0 – volume: 330 start-page: 1066 year: 2010 ident: 90_CR54 publication-title: Science doi: 10.1126/science.1194396 |
| SSID | ssj0000392740 |
| Score | 2.172533 |
| Snippet | Purpose
The thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves’ disease. The TSHR is composed... The thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves' disease. The TSHR is composed of: a... PurposeThe thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves’ disease. The TSHR is composed... PURPOSEThe thyroid-stimulating hormone receptor (TSHR) is the target autoantigen for TSHR-stimulating autoantibodies in Graves' disease. The TSHR is composed... |
| SourceID | pubmedcentral proquest pubmed crossref springer |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 2 |
| SubjectTerms | Autoantibodies Biomedical and Life Sciences Biomedicine Crystal structure Follicle-stimulating hormone G protein-coupled receptors Graves' disease Immunology Leucine Luteinizing hormone Original Original Article Thyroid Thyroid gland Thyroid-stimulating hormone Thyroid-stimulating hormone receptors Transmembrane domains |
| SummonAdditionalLinks | – databaseName: Springer Nature Consortium list (Orbis Cascade Alliance) dbid: RSV link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1La9wwEB7KtoFe-kjaxG1aFOipxSBLlmUfS0nYQ1hKdhNyM5IskYWud9lHIf8-I_mxbJIG0rMl2xqNNN9oZj4BfMsKRatKuFhzY-PUZirW2rhYFUZaryJCBcr8czka5dfXxe-2jnvVZbt3IcmwU2-L3TjaOnR90QOmBY3R5XmJ1i739zVcjK_6gxWKFl-GQkhGuS8fo6KLZj72ll179ABkPsyVvBcwDXbo7O1_jeAdvGlhJ_nZ6Ml7eGHrfdhrLqK8PcDNNdDIbpaWqLoivtihOaolc0cQIpLJeEhwb7QLdNHJ2tu3mZ2ho11bUs1nalp_gMuz08mvYdxerhCbVNJ1zHgmuDLSucQwV1Dn09W00JVUuWKOJdo5kSaJZlqpospxTrU0iZbKIORTjH-EQT2v7REQpTKbCqFTjj3yiqmKo9OHSMIFQjkdAe1EXJqWedxfgPGn3HIme8mUPtvMS6ZMIvjed1k0tBtPNT7u5q1sV-CqROghufRoJIKT_jGuHR8QQenMN6sSvduMZznjaQSHzTT3X_PEimjVZQRyRwH6Bp6Xe_dJPb0J_Nwi4RkCuwh-dGqw_a1_DuLTs1p_htfM44uQV3MMA1QS-wVemb_r6Wr5NSyIO51BBN8 priority: 102 providerName: Springer Nature |
| Title | Structure and activation of the TSH receptor transmembrane domain |
| URI | https://link.springer.com/article/10.1007/s13317-016-0090-1 https://www.ncbi.nlm.nih.gov/pubmed/27921237 https://www.proquest.com/docview/2427371853 https://www.proquest.com/docview/1846368234 https://pubmed.ncbi.nlm.nih.gov/PMC5136658 |
| Volume | 8 |
| WOSCitedRecordID | wos000390887200002&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: ProQuest Biological Science Database (NC LIVE) customDbUrl: eissn: 2038-3274 dateEnd: 20211231 omitProxy: false ssIdentifier: ssj0000392740 issn: 2038-0305 databaseCode: M7P dateStart: 20100501 isFulltext: true titleUrlDefault: http://search.proquest.com/biologicalscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 2038-3274 dateEnd: 20211231 omitProxy: false ssIdentifier: ssj0000392740 issn: 2038-0305 databaseCode: BENPR dateStart: 20100501 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: Publicly Available Content Database customDbUrl: eissn: 2038-3274 dateEnd: 20211231 omitProxy: false ssIdentifier: ssj0000392740 issn: 2038-0305 databaseCode: PIMPY dateStart: 20100501 isFulltext: true titleUrlDefault: http://search.proquest.com/publiccontent providerName: ProQuest – providerCode: PRVAVX databaseName: Springer Standard Collection customDbUrl: eissn: 2038-3274 dateEnd: 20211231 omitProxy: false ssIdentifier: ssj0000392740 issn: 2038-0305 databaseCode: RSV dateStart: 20100501 isFulltext: true titleUrlDefault: https://link.springer.com/search?facet-content-type=%22Journal%22 providerName: Springer Nature |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9QwEB7RFiQu5VkIlJWROIEsEjuJkxMC1KpIsIragpZT5KdYiU2W7rYS_56x81gtFb1wtGwr8Xg8L4-_AXiVlzI2JnNUcW1panNJldKOylIL61kkkwEy_7OYTovZrKz6gNuqT6scZGIQ1KbVPkb-FlWJ4MJrl3fLX9RXjfK3q30JjR3Y8ygJLKTuVWOMJUblL8KbSBZz_5IszoaLzfB6jqPyRF8aXeq4jGmyrZqu2ZvX0yb_ujsNKun43v8u5j7s98Yoed9xzwO4ZZuHcKcrT_n7EYrcAC57eWGJbAzxTyC6AC5pHUHDkZyfnRCUmHaJjjtZe623sAt0vxtLTLuQ8-YxfD0-Ov94QvuSC1SnIl5TxvOMSy2cSzRzZex8EpvKlBGykMyxRDmXpUmimJKyNAXutBI6UUJqNAQl4wew27SNfQpEytymWaZSjjMKw6Th6AqifeECzJyKIB6oXesej9yXxfhZb5CU_QbVPgfNb1CdRPB6nLLswDhuGnw40L7uz-Wq3hA-gpdjN54of02C1GkvVzX6vDnPC8bTCJ50Oz5-zcMtoq4XEYgtXhgHeLTu7Z5m_iOgdmcJz9Hci-DNwDWb3_rnIp7dvIjncJd5MyOk1xzCLnKFfQG39dV6vrqYwI6YFRPY-3A0rU4n4Whgq_r0pfqOrdOzb38AqDIU6w |
| linkProvider | ProQuest |
| linkToHtml | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9NAEB5VKYheeD8MBRYJLiALe9f22geEEFAlahpFIkjl5O6ud0Wkxg5JCuqf4jcy40eiUNFbD5x8sC17vZ9nvtmd-QbgZZKpoChi52thrB_ZRPlaG-erzEhLEIlVLZk_lKNRenycjXfgd1cLQ2mVnU2sDXVRGVojf4uuRApJ3uX9_IdPXaNod7VrodHA4tCe_8KQbflu8Ann9xXnB58nH_t-21XAN5EMVj4XSSyUkc6FhrsscJSnpWNdSJUq7nionYujMNRcK5UVKQ5GSxNqqQxyHUVCB2jydyMCew92x4Oj8bf1qk6AdEPWVZg8EFS7FsTdVmpdryfQXWP0jkF8kAV-uO0MLzDci4maf-3W1k7w4Nb_9vluw82WbrMPzf9xB3ZseReuNw04z--hU6nlc88WlqmyYFTk0SxRs8oxpMZs8qXP0CfY-apasBX59ZmdaTxaVlQzNS3vw9cref8H0Cur0j4CplRiozjWkcA70oKrQmCwiwzK1UJ62oOgm93ctIrr1PjjNN9oRRMgcsqyI0DkoQev17fMG7mRyy7e7-Y6by3PMt9MtAcv1qfRZtBGEH6d6myZY1SfiCTlIvLgYYOw9dNIUBLZjPRAbmFvfQHpkW-fKaffa13yOBQJEloP3nQo3bzWPwfx-PJBPIcb_cnRMB8ORodPYI8TqaqTifahhwixT-Ga-bmaLhfP2l-RwclVw_cPpKFvrg |
| linkToPdf | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9QwEB6h8hCX8obQAkbiBIrq2HGcHCtgVUS1qtSCeov8FCux2VV3i8S_70xeq6WAhDjHTuLx2PONZ-YzwJuiMtx7FVMrXUjzUJjUWhdTUzkdSEWUaSnzj_V0Wp6fVyf9PaerIdt9CEl2NQ3E0tSsD5Y-HmwK3yTaPXSD0RvmFU_R_bmZUx49ueunX8dDFo7WX7dFkYJLKiXjaohs_u4t27bpGuC8njf5S_C0tUmTe_89mvuw28NRdtjpzwO4EZqHcLu7oPLnI9x0W3rZy4vATOMZFUF0R7hsERlCR3Z2esRwzwxLdN3ZmuzePMzRAW8C84u5mTWP4cvk49n7o7S_dCF1uebrVMhCSeN0jJkTseKR0tissl6b0ogoMhujyrPMCmtM5Uuca6tdZrVxCAWNkE9gp1k04RkwY4qQK2VziT1KL4yX6Awiwogt0ZxNgA_irl3PSE4XY3yvN1zKJJmastBIMnWWwNuxy7Kj4_hb4_1hDut-Za5qhCRaakIpCbweH-OaokAJSmdxuarR6y1kUQqZJ_C0m_Lxa0S4iNZeJ6C3lGFsQHzd20-a2beWt1tlskDAl8C7QSU2v_XHQTz_p9av4M7Jh0l9_Gn6eQ_uCoIgberNPuygvoQXcMv9WM9WFy_bdXIFWkQQpw |
| 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=Structure+and+activation+of+the+TSH+receptor+transmembrane+domain&rft.jtitle=Autoimmunity+highlights&rft.au=N%C3%BA%C3%B1ez+Miguel%2C+Ricardo&rft.au=Sanders%2C+Jane&rft.au=Furmaniak%2C+Jadwiga&rft.au=Smith%2C+Bernard+Rees&rft.date=2017-12-01&rft.issn=2038-0305&rft.volume=8&rft.issue=1&rft.spage=2&rft.epage=2&rft_id=info:doi/10.1007%2Fs13317-016-0090-1&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2038-0305&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2038-0305&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2038-0305&client=summon |