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Structural basis of Hsp90 function
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posted on 2023-06-09, 09:09 authored by Chrisostomos ProdromouChrisostomos Prodromou, Laurence PearlLaurence PearlHeat shock protein 90 (Hsp90) stands at the crossroads of many signaling pathways responsible for cell proliferation, differentiation, cell homeostasis and apoptosis. Consequently, it is no surprise that Hsp90 is associated with all the six hallmarks of cancer and has become a prime anticancer target. Central to the Hsp90 mechanism is its ATPase activity, which is coupled to a conformational cycle involving a complex set of structural changes that involve all Hsp90 domains. The mechanism by which Hsp90 activates “client” protein is still poorly understood. However, there has been excellent progress on elucidating the molecular details of the complex structural changes required for Hsp90’s catalytically active state and how this activity is influenced by a variety of co-chaperones and client proteins. This review aims to bring together structural investigations that have so far contributed to our understanding of this ATPase-coupled conformational cycle and how this activity is regulated and ultimately has become the prime target for Hsp90 drugs.
History
Publication status
- Published
Publisher
RSC PublishingPage range
37-64Pages
28.0Book title
Inhibitors of molecular chaperones as therapeutic agentsPlace of publication
Cambridge, UKISBN
9781849736664Series
RSC drug discovery; No. 37Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Editors
David Rotella, Zhenhai Gao, Timothy D MachajewskiLegacy Posted Date
2017-12-04Usage metrics
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