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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
Full text not available from this repository.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 |