Visualizing the transiently populated closed-state of human HSP90 ATP binding domain

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
Format: Article
Language:English
Published: Nature Portfolio 2022-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-35399-8

Internet

https://doi.org/10.1038/s41467-022-35399-8

Similar Items