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000140876 0247_ $$2doi$$a10.1002/pro.3678
000140876 0247_ $$2pmid$$apmid:31299134
000140876 0247_ $$2pmc$$apmc:PMC6699087
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000140876 0247_ $$2ISSN$$a1469-896X
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000140876 037__ $$aDZNE-2020-07198
000140876 041__ $$aEnglish
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000140876 1001_ $$0P:(DE-2719)2810826$$aOroz, Javier$$b0$$eFirst author$$udzne
000140876 245__ $$aDynamic Aha1 co-chaperone binding to human Hsp90.
000140876 260__ $$aBethesda, Md.$$bProtein Society$$c2019
000140876 264_1 $$2Crossref$$3online$$bWiley$$c2019-08-06
000140876 264_1 $$2Crossref$$3print$$bWiley$$c2019-09-01
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000140876 520__ $$aHsp90 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.
000140876 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000140876 542__ $$2Crossref$$i2019-08-06$$uhttp://creativecommons.org/licenses/by/4.0/
000140876 542__ $$2Crossref$$i2019-08-06$$uhttp://doi.wiley.com/10.1002/tdm_license_1.1
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000140876 650_2 $$2MeSH$$aAllosteric Regulation
000140876 650_2 $$2MeSH$$aBinding Sites
000140876 650_2 $$2MeSH$$aHSP90 Heat-Shock Proteins: chemistry
000140876 650_2 $$2MeSH$$aHSP90 Heat-Shock Proteins: metabolism
000140876 650_2 $$2MeSH$$aHumans
000140876 650_2 $$2MeSH$$aModels, Molecular
000140876 650_2 $$2MeSH$$aMolecular Chaperones: chemistry
000140876 650_2 $$2MeSH$$aMolecular Chaperones: metabolism
000140876 650_2 $$2MeSH$$aMolecular Weight
000140876 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000140876 650_2 $$2MeSH$$aProtein Binding
000140876 650_2 $$2MeSH$$aProtein Conformation
000140876 7001_ $$aBlair, Laura J$$b1
000140876 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b2$$eLast author$$udzne
000140876 77318 $$2Crossref$$3journal-article$$a10.1002/pro.3678$$b : Wiley, 2019-08-06$$n9$$p1545-1551$$tProtein Science$$v28$$x0961-8368$$y2019
000140876 773__ $$0PERI:(DE-600)2000025-X$$a10.1002/pro.3678$$gVol. 28, no. 9, p. 1545 - 1551$$n9$$p1545-1551$$q28:9<1545 - 1551$$tProtein science$$v28$$x0961-8368$$y2019
000140876 8564_ $$uhttps://pub.dzne.de/record/140876/files/5361.pdf$$yOpenAccess
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000140876 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC6699087
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