A molecular switch regulating transcriptional repression and activation of PPARγ
Structural studies of nuclear receptor transcription factors revealed that nearly all nuclear receptors share a conserved helix 12 dependent transcriptional activation mechanism. Here the authors present two crystal structures of peroxisome proliferator-activated receptor gamma (PPARγ) in an inverse...
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2020-02-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-14750-x |
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doaj-9d32e7db99b24a56b787934b31a561302021-05-11T08:56:39ZengNature Publishing GroupNature Communications2041-17232020-02-0111111410.1038/s41467-020-14750-xA molecular switch regulating transcriptional repression and activation of PPARγJinsai Shang0Sarah A. Mosure1Jie Zheng2Richard Brust3Jared Bass4Ashley Nichols5Laura A. Solt6Patrick R. Griffin7Douglas J. Kojetin8Department of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteSummer Undergraduate Research Fellows (SURF) program, The Scripps Research InstituteDepartment of Immunology and Microbiology, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteStructural studies of nuclear receptor transcription factors revealed that nearly all nuclear receptors share a conserved helix 12 dependent transcriptional activation mechanism. Here the authors present two crystal structures of peroxisome proliferator-activated receptor gamma (PPARγ) in an inverse agonist/corepressor-bound transcriptionally repressive conformation, where helix 12 is located within the orthosteric ligand-binding pocket instead, and discuss mechanistic implications.https://doi.org/10.1038/s41467-020-14750-x |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jinsai Shang Sarah A. Mosure Jie Zheng Richard Brust Jared Bass Ashley Nichols Laura A. Solt Patrick R. Griffin Douglas J. Kojetin |
spellingShingle |
Jinsai Shang Sarah A. Mosure Jie Zheng Richard Brust Jared Bass Ashley Nichols Laura A. Solt Patrick R. Griffin Douglas J. Kojetin A molecular switch regulating transcriptional repression and activation of PPARγ Nature Communications |
author_facet |
Jinsai Shang Sarah A. Mosure Jie Zheng Richard Brust Jared Bass Ashley Nichols Laura A. Solt Patrick R. Griffin Douglas J. Kojetin |
author_sort |
Jinsai Shang |
title |
A molecular switch regulating transcriptional repression and activation of PPARγ |
title_short |
A molecular switch regulating transcriptional repression and activation of PPARγ |
title_full |
A molecular switch regulating transcriptional repression and activation of PPARγ |
title_fullStr |
A molecular switch regulating transcriptional repression and activation of PPARγ |
title_full_unstemmed |
A molecular switch regulating transcriptional repression and activation of PPARγ |
title_sort |
molecular switch regulating transcriptional repression and activation of pparγ |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2020-02-01 |
description |
Structural studies of nuclear receptor transcription factors revealed that nearly all nuclear receptors share a conserved helix 12 dependent transcriptional activation mechanism. Here the authors present two crystal structures of peroxisome proliferator-activated receptor gamma (PPARγ) in an inverse agonist/corepressor-bound transcriptionally repressive conformation, where helix 12 is located within the orthosteric ligand-binding pocket instead, and discuss mechanistic implications. |
url |
https://doi.org/10.1038/s41467-020-14750-x |
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