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Structure and in vivo function of Hsp90

journal contribution
posted on 2023-06-08, 14:43 authored by Laurence PearlLaurence Pearl, Chrisostomos ProdromouChrisostomos Prodromou
Until recently, Hsp90 was one of the least well understood of the molecular chaperones, but considerable progress is now being made in unravelling its biochemistry. Hsp90 has now been shown to possess an inherent ATPase that is essential for the activation of authentic 'client' proteins in vivo and in vitro. The molecular detail of Hsp90's interactions with co-chaperones is also becoming clearer and the identification of key roles in assembling regulatory and signalling pathways has made it a target for anticancer drug development. Despite this, a clear understanding of how Hsp90 contributes to the folding and/or activation of its client proteins remains some way off.

History

Publication status

  • Published

Journal

Current Opinion in Structural Biology

ISSN

0959-440X

Publisher

Elsevier

Issue

1

Volume

10

Page range

46-51

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2015-02-25