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Article

Hsp90 is regulated by a switch point in the C-terminal domain.

EMBO reports - 1 Oct 2009

Retzlaff Marco, Stahl Michael, Eberl H Christian, Lagleder Stephan, Beck Jürgen, Kessler Horst, Buchner Johannes

Abstract excerpt

Heat shock protein 90 (Hsp90) is an abundant, dimeric ATP-dependent molecular chaperone, and ATPase activity is essential for its in vivo functions. S-nitrosylation of a residue located in the carboxy-terminal domain has been shown to affect Hsp90 activity in vivo. To understand how variation of a specific amino acid far away from the amino-terminal ATP-binding site regulates Hsp90 functions, we mutated the...

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Share to Adenosine Triphosphatases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19696785
DOI: 10.1038/embor.2009.153
PMCID: PMC2759728

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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