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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. © 2019 The Authors. Protein Science published by Wiley Periodicals, Inc. on behalf of The Protein Society.


Javier Oroz, Laura J Blair, Markus Zweckstetter. Dynamic Aha1 co-chaperone binding to human Hsp90. Protein science : a publication of the Protein Society. 2019 Sep;28(9):1545-1551

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PMID: 31299134

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