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.
Bibliographic Details
| Main Authors: |
Faustine Henot,
Elisa Rioual,
Adrien Favier,
Pavel Macek,
Elodie Crublet,
Pierre Josso,
Bernhard Brutscher,
Matthias Frech,
Pierre Gans,
Claire Loison,
Jerome Boisbouvier |
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| Format: | Article
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| Language: | English |
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| Published: |
Nature Portfolio
2022-12-01
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| Series: | Nature Communications
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| Online Access: | https://doi.org/10.1038/s41467-022-35399-8
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