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The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins.

Abstract:

The action of the molecular chaperone Hsp90 is essential for the activation and assembly of an increasing number of client proteins. This function of Hsp90 has been proposed to be governed by conformational changes driven by ATP binding and hydrolysis. Association of co-chaperones and client proteins regulate the ATPase activity of Hsp90. Here, we have examined the inhibition of the ATPase activity of human Hsp90beta by one such co-chaperone, human p23. We demonstrate that human p23 interacts...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2005.11.085

Authors


McLaughlin, SH More by this author
Nielsen, PR More by this author
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Journal:
Journal of molecular biology
Volume:
356
Issue:
3
Pages:
746-758
Publication date:
2006-02-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:cc4c51f6-bf0c-4c3c-a278-b93b66c94475
Source identifiers:
59283
Local pid:
pubs:59283

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