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Article

Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.

The Journal of biological chemistry - 25 Jul 2008

Cunningham Christian N, Krukenberg Kristin A, Agard David A

Abstract excerpt

Nucleotide-dependent conformational changes of the constitutively dimeric molecular chaperone Hsp90 are integral to its molecular mechanism. Recent full-length crystal structures (Protein Data Bank codes 2IOQ, 2CG9, AND 2IOP) of Hsp90 homologs reveal large scale quaternary domain rearrangements upon the addition of nucleotides. Although previous work has shown the importance of C-terminal domain dimerization for...

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Identifiers

PMID: 18492664
DOI: 10.1074/jbc.M800046200
PMCID: PMC2475720

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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