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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 Pearl
Hsp90 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 Biology

ISSN

1072-8368

Publisher

Nature Publishing Group

Issue

6

Volume

4

Page range

477-482

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2015-02-24