Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ

The repressive states of peroxisome proliferator-activated receptor γ (PPARγ) are ill-defined, despite nuclear receptors being a major drug target. Here authors demonstrate multiple structurally distinct repressive states, providing a structural rationale for ligand bias in a nuclear receptor.

Bibliographic Details
Main Authors: Zahra Heidari, Ian M. Chrisman, Michelle D. Nemetchek, Scott J. Novick, Anne-Laure Blayo, Trey Patton, Desiree E. Mendes, Philippe Diaz, Theodore M. Kamenecka, Patrick R. Griffin, Travis S. Hughes
Format: Article
Language:English
Published: Nature Publishing Group 2019-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-13768-0
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spelling doaj-27b2fda7dc814baabc2b2a797db6f9452021-05-11T11:30:19ZengNature Publishing GroupNature Communications2041-17232019-12-0110111410.1038/s41467-019-13768-0Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγZahra Heidari0Ian M. Chrisman1Michelle D. Nemetchek2Scott J. Novick3Anne-Laure Blayo4Trey Patton5Desiree E. Mendes6Philippe Diaz7Theodore M. Kamenecka8Patrick R. Griffin9Travis S. Hughes10Department of Biomedical and Pharmaceutical Sciences, University of MontanaCenter for Biomolecular Structure and Dynamics, University of MontanaCenter for Biomolecular Structure and Dynamics, University of MontanaDepartment of Molecular Medicine, The Scripps Research InstituteDepartment of Molecular Medicine, The Scripps Research InstituteDepartment of Biomedical and Pharmaceutical Sciences, University of MontanaDepartment of Biomedical and Pharmaceutical Sciences, University of MontanaDepartment of Biomedical and Pharmaceutical Sciences, University of MontanaDepartment of Molecular Medicine, The Scripps Research InstituteDepartment of Molecular Medicine, The Scripps Research InstituteDepartment of Biomedical and Pharmaceutical Sciences, University of MontanaThe repressive states of peroxisome proliferator-activated receptor γ (PPARγ) are ill-defined, despite nuclear receptors being a major drug target. Here authors demonstrate multiple structurally distinct repressive states, providing a structural rationale for ligand bias in a nuclear receptor.https://doi.org/10.1038/s41467-019-13768-0
collection DOAJ
language English
format Article
sources DOAJ
author Zahra Heidari
Ian M. Chrisman
Michelle D. Nemetchek
Scott J. Novick
Anne-Laure Blayo
Trey Patton
Desiree E. Mendes
Philippe Diaz
Theodore M. Kamenecka
Patrick R. Griffin
Travis S. Hughes
spellingShingle Zahra Heidari
Ian M. Chrisman
Michelle D. Nemetchek
Scott J. Novick
Anne-Laure Blayo
Trey Patton
Desiree E. Mendes
Philippe Diaz
Theodore M. Kamenecka
Patrick R. Griffin
Travis S. Hughes
Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ
Nature Communications
author_facet Zahra Heidari
Ian M. Chrisman
Michelle D. Nemetchek
Scott J. Novick
Anne-Laure Blayo
Trey Patton
Desiree E. Mendes
Philippe Diaz
Theodore M. Kamenecka
Patrick R. Griffin
Travis S. Hughes
author_sort Zahra Heidari
title Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ
title_short Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ
title_full Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ
title_fullStr Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ
title_full_unstemmed Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ
title_sort definition of functionally and structurally distinct repressive states in the nuclear receptor pparγ
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-12-01
description The repressive states of peroxisome proliferator-activated receptor γ (PPARγ) are ill-defined, despite nuclear receptors being a major drug target. Here authors demonstrate multiple structurally distinct repressive states, providing a structural rationale for ligand bias in a nuclear receptor.
url https://doi.org/10.1038/s41467-019-13768-0
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