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

Academic Article
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Overview

authors

  • Li, X.
  • Anderson, M.
  • Collin, D.
  • Muegge, I.
  • Wan, J.
  • Brennan, D.
  • Kugler, S.
  • Terenzio, D.
  • Kennedy, C.
  • Lin, S.
  • Labadia, M. E.
  • Cook, B.
  • Hughes, Robert Owen
  • Farrow, N. A.

publication date

  • July 2017

journal

  • Journal of Biological Chemistry  Journal

subject areas

  • Anti-Inflammatory Agents, Non-Steroidal
  • Apoproteins
  • Binding Sites
  • Binding, Competitive
  • Cells, Cultured
  • Drug Inverse Agonism
  • Genes, Reporter
  • HEK293 Cells
  • Humans
  • Interleukin-17
  • Ligands
  • Models, Molecular
  • Molecular Conformation
  • Nuclear Receptor Subfamily 1, Group F, Member 3
  • Peptide Fragments
  • Phenylalanine
  • Phenylurea Compounds
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Protein Refolding
  • Protein Stability
  • Recombinant Fusion Proteins
  • Th17 Cells
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Research

keywords

  • crystal structure
  • drug discovery
  • nuclear magnetic resonance (NMR)
  • nuclear receptor
  • protein drug interaction
  • retinoid acid receptor-related orphan receptor t (RORt)
  • x-ray crystallography
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Identity

PubMed Central ID

  • PMC5512059

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M117.789024

PubMed ID

  • 28546429
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Additional Document Info

start page

  • 11618

end page

  • 11630

volume

  • 292

issue

  • 28

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