Comment in:

Nat Struct Biol. 1997 Jun;4(6):430-4.

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

Department of Biochemistry and Molecular Biology, University College London, UK.

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.

PMID: 9187656 [PubMed - indexed for MEDLINE]