A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

Prodromou, Chrisostomos, Roe, S Mark, Piper, Peter W and Pearl, Laurence H (1997) A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature Structural Biology, 4 (6). pp. 477-482. ISSN 1072-8368

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Abstract

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.

Item Type: Article
Keywords: Amino Acid Sequence Binding Sites Conserved Sequence Crystallography, X-Ray Dimerization Fungal Proteins/chemistry/genetics/metabolism HSP90 Heat-Shock Proteins/*chemistry/genetics/*metabolism Hydrogen Bonding Ligands Models, Molecular Peptides/chemistry/metabolism Protein Conformation Protein Folding Saccharomyces cerevisiae/chemistry
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science > QD Chemistry > QD0241 Organic chemistry > QD0415 Biochemistry
Q Science > QD Chemistry > QD0901 Crystallography
Depositing User: Chrisostomos Prodromou
Date Deposited: 24 Feb 2015 17:49
Last Modified: 24 Feb 2015 17:49
URI: http://sro.sussex.ac.uk/id/eprint/44365
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