Structural studies unravel the active conformation of apo RORγt nuclear receptor and a common inverse agonism of two diverse classes of RORγt inhibitors

Li, X, Anderson, M, Collin, D et al. (11 more authors) (2017) Structural studies unravel the active conformation of apo RORγt nuclear receptor and a common inverse agonism of two diverse classes of RORγt inhibitors. Journal of Biological Chemistry, 292 (28). pp. 11618-11630. ISSN 0021-9258

Abstract

Metadata

Authors/Creators:
  • Li, X
  • Anderson, M
  • Collin, D
  • Muegge, I
  • Wan, J
  • Brennan, D
  • Kugler, S
  • Terenzio, D
  • Kennedy, C
  • Lin, S
  • Labadia, ME
  • Cook, B
  • Hughes, R
  • Farrow, NA
Copyright, Publisher and Additional Information: © 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. This is an open access article under the CC BY license.
Keywords: crystal structure; drug discovery; nuclear magnetic resonance (NMR); nuclear receptor; protein drug interaction; x-ray crystallography; retinoid acid receptor-related orphan receptor γt (RORγt)
Dates:
  • Accepted: 30 March 2017
  • Published: 14 July 2017
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds)
Depositing User: Symplectic Publications
Date Deposited: 11 Jun 2021 08:29
Last Modified: 11 Jun 2021 08:29
Status: Published
Publisher: Elsevier
Identification Number: https://doi.org/10.1074/jbc.m117.789024

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