Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle

p23 is a co-chaperone of Hsp90 but its mode of action is mechanistically not well understood. Here, the authors combine in vitro and yeast in vivo assays, biochemical measurements and NMR experiments to characterize p23 and identify two conserved helical elements in the intrinsically disordered C-te...

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Bibliographic Details
Main Authors: Maximilian M. Biebl, Abraham Lopez, Alexandra Rehn, Lee Freiburger, Jannis Lawatscheck, Birgit Blank, Michael Sattler, Johannes Buchner
Format: Article
Language:English
Published: Nature Publishing Group 2021-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-21063-0