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• W2152226677 endingPage "1410" @default.
• W2152226677 startingPage "1402" @default.
• W2152226677 abstract "Hsp90 is a molecular chaperone essential for the activation and assembly of many key eukaryotic signalling and regulatory proteins. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series of dynamic multiprotein complexes, linked to Hsp90 conformationally coupled ATPase cycle. The co-chaperones Aha1 and Hch1 bind to Hsp90 and stimulate its ATPase activity. Biochemical analysis shows that this activity is dependent on the N-terminal domain of Aha1, which interacts with the central segment of Hsp90. The structural basis for this interaction is revealed by the crystal structure of the N-terminal domain (1-153) of Aha1 (equivalent to the whole of Hch1) in complex with the middle segment of Hsp90 (273-530). Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone." @default.
• W2152226677 created "2016-06-24" @default.
• W2152226677 creator A5070655107 @default.
• W2152226677 date "2004-03-24" @default.
• W2152226677 modified "2023-10-10" @default.
• W2152226677 title "Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery" @default.
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• W2152226677 doi "https://doi.org/10.1038/sj.emboj.7600141" @default.
• W2152226677 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/381413" @default.
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