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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 ProdromouUntil 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 BiologyISSN
0959-440XPublisher
ElsevierExternal DOI
Issue
1Volume
10Page range
46-51Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2015-02-25Usage metrics
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No categories selectedKeywords
Adenosine Triphosphate/physiologyAllosteric RegulationAnimalsBacterial Proteins/chemistry/physiologyBenzoquinonesHSP90 Heat-Shock Proteins/antagonists & inhibitors/chemistry/*physiologyHumansLactamsMacrocyclicMacromolecular SubstancesModelsBiologicalMolecularProtein BindingQuinones/pharmacologySignal Transduction/physiologyStructure-Activity Relationship
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