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A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
journal contribution
posted on 2023-06-08, 14:43 authored by Chrisostomos ProdromouChrisostomos Prodromou, S Mark Roe, Peter W Piper, Laurence PearlLaurence PearlHsp90 is a highly specific chaperone for many signal transduction proteins, including steroid hormone receptors and a broad range of protein kinases. The crystal structure of the N-terminal domain of the yeast Hsp90 reveals a dimeric structure based on a highly twisted sixteen stranded beta-sheet, whose topology suggests a possible 30-domain-swapped structure for the intact Hsp90 dimer. The opposing faces of the beta-sheets in the dimer define a potential peptide-binding cleft, suggesting that the N-domain may serve as a molecular 'clamp' in the binding of ligand proteins to Hsp90.
History
Publication status
- Published
Journal
Nature Structural BiologyISSN
1072-8368Publisher
Nature Publishing GroupExternal DOI
Issue
6Volume
4Page range
477-482Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2015-02-24Usage metrics
Categories
Keywords
Amino Acid SequenceBinding SitesConserved SequenceX-RayDimerizationFungal Proteins/chemistry/genetics/metabolismHSP90 Heat-Shock Proteins/*chemistry/genetics/*metabolismHydrogen BondingLigandsModelsMolecularPeptides/chemistry/metabolismProtein ConformationProtein FoldingSaccharomyces cerevisiae/chemistry
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