Identification of an allosteric binding site for RORγt inhibition

RORγt is critical for the differentiation and proliferation of Th17 cells associated with several chronic autoimmune diseases. We report the discovery of a novel allosteric binding site on the nuclear receptor RORγt. Co-crystallization of the ligand binding domain (LBD) of RORγt with a series of sma...

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Veröffentlicht in:	Nature communications Jg. 6; H. 1; S. 8833
Hauptverfasser:	Scheepstra, Marcel, Leysen, Seppe, van Almen, Geert C., Miller, J. Richard, Piesvaux, Jennifer, Kutilek, Victoria, van Eenennaam, Hans, Zhang, Hongjun, Barr, Kenneth, Nagpal, Sunil, Soisson, Stephen M., Kornienko, Maria, Wiley, Kristen, Elsen, Nathaniel, Sharma, Sujata, Correll, Craig C., Trotter, B. Wesley, van der Stelt, Mario, Oubrie, Arthur, Ottmann, Christian, Parthasarathy, Gopal, Brunsveld, Luc
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	London Nature Publishing Group UK 07.12.2015 Nature Publishing Group
Schlagworte:	60 APPLIED LIFE SCIENCES 631/45/612/388 631/57/2272 692/699/2743/1313 692/700/565/1331 82 82/80 82/83 Allosteric Site Animals Cell Differentiation Humanities and Social Sciences Humans Interleukin-17 - chemistry Interleukin-17 - metabolism Ligands Mice multidisciplinary Nuclear Receptor Subfamily 1, Group F, Member 3 - chemistry Nuclear Receptor Subfamily 1, Group F, Member 3 - genetics Nuclear Receptor Subfamily 1, Group F, Member 3 - metabolism Protein Structure, Tertiary Science Science (multidisciplinary) Th17 Cells - chemistry Th17 Cells - metabolism
ISSN:	2041-1723, 2041-1723
Online-Zugang:	Volltext
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