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RORγ Structural Plasticity and Druggability.

Mian Huang1, Shelby Bolin2, Hannah Miller1

  • 1Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA.

International Journal of Molecular Sciences
|July 31, 2020
PubMed
Summary

Retinoic acid receptor-related orphan receptor gamma (RORγ) is a key regulator of inflammation and autoimmune diseases. Its structural plasticity enhances its potential as a drug target, particularly for allosteric ligands.

Keywords:
RORγallosteric binding pocketdruggabilityorthosteric binding pocketplasticity

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Area of Science:

  • Immunology
  • Structural Biology
  • Pharmacology

Background:

  • Retinoic acid receptor-related orphan receptor gamma (RORγ) is a transcription factor controlling IL-17 production in T helper 17 (Th17) cells.
  • RORγ's role in IL-17-mediated autoimmune diseases and potential anticancer applications makes it a significant drug target.

Purpose of the Study:

  • To review the dynamic properties and plasticity of RORγ's binding sites.
  • To examine how structural flexibility influences RORγ druggability, focusing on allosteric ligand interactions.

Main Methods:

  • Analysis of over 100 published crystal structures of RORγ with agonists and inverse agonists.
  • Examination of simulated models to understand dynamic properties and binding site plasticity.
  • Discussion of allosteric ligand effects on the orthosteric binding site.

Main Results:

  • RORγ exhibits significant structural plasticity in its orthosteric and allosteric binding sites.
  • High structural plasticity is correlated with enhanced druggability of RORγ.
  • Allosteric ligands may influence the orthosteric binding site.

Conclusions:

  • The structural plasticity of RORγ favors its druggability, especially for allosteric modulators.
  • Understanding RORγ dynamics is crucial for developing targeted therapies for autoimmune diseases and cancer.