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Article

Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle.

The Journal of biological chemistry - 10 Dec 2004

Siligardi Giuliano, Hu Bin, Panaretou Barry, Piper Peter W, Pearl Laurence H, Prodromou Chrisostomos

Abstract excerpt

ATP hydrolysis by the Hsp90 molecular chaperone requires a connected set of conformational switches triggered by ATP binding to the N-terminal domain in the Hsp90 dimer. Central to this is a segment of the structure, which closes like a "lid" over bound ATP, promoting N-terminal dimerization and assembly of a competent active site. Hsp90 mutants that influence these conformational switches have strong effects on...

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Identifiers

PMID: 15466438
DOI: 10.1074/jbc.M410562200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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