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Article

N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.

The Journal of biological chemistry - 22 Nov 2002

Richter Klaus, Reinstein Jochen, Buchner Johannes

Abstract excerpt

Hsp90 is an abundant molecular chaperone involved in a variety of cellular processes ranging from signal transduction to viral replication. The function of Hsp90 has been shown to be dependent on its ability to hydrolyze ATP, and in vitro studies suggest that the dimeric nature of Hsp90 is critical for this activity. ATP binding occurs at the N-terminal domains of the Hsp90 dimer, whereas the main dimerization...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 12235160
DOI: 10.1074/jbc.M208457200

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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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N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.PMID 12235160Read ↗

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