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

Nat Struct Biol. 1997 Jun;4(6):477-82. doi: 10.1038/nsb0697-477.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Conserved Sequence
  • Crystallography, X-Ray
  • Dimerization
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • HSP90 Heat-Shock Proteins / chemistry*
  • HSP90 Heat-Shock Proteins / genetics
  • HSP90 Heat-Shock Proteins / metabolism*
  • Hydrogen Bonding
  • Ligands
  • Models, Molecular
  • Peptides / chemistry
  • Peptides / metabolism
  • Protein Conformation
  • Protein Folding
  • Saccharomyces cerevisiae / chemistry

Substances

  • Fungal Proteins
  • HSP90 Heat-Shock Proteins
  • Ligands
  • Peptides