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 |