Dynamic Aha1 Co-Chaperone Binding to Human Hsp90.

08:00 EDT 12th July 2019 | BioPortfolio

Summary of "Dynamic Aha1 Co-Chaperone Binding to Human Hsp90."

Hsp90 is an essential chaperone that requires large allosteric changes to determine its ATPase activity and client binding. The co-chaperone Aha1, which is the major ATPase stimulator in eukaryotes, is important for regulation of Hsp90's allosteric timing. Little is known, however, about the structure of the Hsp90/Aha1 complex. Here, we characterize the solution structure of unmodified human Hsp90/Aha1 complex using NMR spectroscopy. We show that the 214-kDa complex forms by a two-step binding mechanism and adopts multiple conformations in the absence of nucleotide. Aha1 induces structural changes near Hsp90's nucleotide-binding site, providing a basis for its ATPase-enhancing activity. Our data reveal important aspects of this pivotal chaperone/co-chaperone interaction and emphasize the relevance of characterizing dynamic chaperone structures in solution. This article is protected by copyright. All rights reserved.


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Name: Protein science : a publication of the Protein Society
ISSN: 1469-896X


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