Visualizing the transiently populated closed-state of human HSP90 ATP binding domain
To refold client proteins, HSP90 chaperone undergoes large structural rearrangements. Here the authors use NMR and molecular simulation and reveal structure and dynamics of a key functionally relevant metastable state of human HSP90α N-terminal domain.
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-35399-8 |
| _version_ | 1811179142717112320 |
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| author | Faustine Henot Elisa Rioual Adrien Favier Pavel Macek Elodie Crublet Pierre Josso Bernhard Brutscher Matthias Frech Pierre Gans Claire Loison Jerome Boisbouvier |
| author_facet | Faustine Henot Elisa Rioual Adrien Favier Pavel Macek Elodie Crublet Pierre Josso Bernhard Brutscher Matthias Frech Pierre Gans Claire Loison Jerome Boisbouvier |
| author_sort | Faustine Henot |
| collection | DOAJ |
| description | To refold client proteins, HSP90 chaperone undergoes large structural rearrangements. Here the authors use NMR and molecular simulation and reveal structure and dynamics of a key functionally relevant metastable state of human HSP90α N-terminal domain. |
| first_indexed | 2024-04-11T06:29:46Z |
| format | Article |
| id | doaj.art-a0e415192adb4a8f825b0f4fa98dd24f |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-11T06:29:46Z |
| publishDate | 2022-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-a0e415192adb4a8f825b0f4fa98dd24f2022-12-22T04:40:11ZengNature PortfolioNature Communications2041-17232022-12-0113111310.1038/s41467-022-35399-8Visualizing the transiently populated closed-state of human HSP90 ATP binding domainFaustine Henot0Elisa Rioual1Adrien Favier2Pavel Macek3Elodie Crublet4Pierre Josso5Bernhard Brutscher6Matthias Frech7Pierre Gans8Claire Loison9Jerome Boisbouvier10Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS)NMR-BioInstitut Lumière Matière, University of Lyon, Université Claude Bernard Lyon 1Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS)Discovery Technologies, Merck KGaAUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS)Institut Lumière Matière, University of Lyon, Université Claude Bernard Lyon 1Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS)To refold client proteins, HSP90 chaperone undergoes large structural rearrangements. Here the authors use NMR and molecular simulation and reveal structure and dynamics of a key functionally relevant metastable state of human HSP90α N-terminal domain.https://doi.org/10.1038/s41467-022-35399-8 |
| spellingShingle | Faustine Henot Elisa Rioual Adrien Favier Pavel Macek Elodie Crublet Pierre Josso Bernhard Brutscher Matthias Frech Pierre Gans Claire Loison Jerome Boisbouvier Visualizing the transiently populated closed-state of human HSP90 ATP binding domain Nature Communications |
| title | Visualizing the transiently populated closed-state of human HSP90 ATP binding domain |
| title_full | Visualizing the transiently populated closed-state of human HSP90 ATP binding domain |
| title_fullStr | Visualizing the transiently populated closed-state of human HSP90 ATP binding domain |
| title_full_unstemmed | Visualizing the transiently populated closed-state of human HSP90 ATP binding domain |
| title_short | Visualizing the transiently populated closed-state of human HSP90 ATP binding domain |
| title_sort | visualizing the transiently populated closed state of human hsp90 atp binding domain |
| url | https://doi.org/10.1038/s41467-022-35399-8 |
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