1AH8

STRUCTURE OF THE ORTHORHOMBIC FORM OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE

Summary for 1AH8

• Entry DOI: 10.2210/pdb1ah8/pdb
• Descriptor: HEAT SHOCK PROTEIN 90, GLYCEROL (3 entities in total)
• Functional Keywords: chaperone, atp-binding, heat shock
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P02829
• Total number of polymer chains: 2
• Total formula weight: 50115.17

Authors

Prodromou, C.,Roe, S.M.,Pearl, L.H. (deposition date: 1997-04-14, release date: 1997-10-22, Last modification date: 2024-04-03)

Primary citation

Prodromou, C.,Roe, S.M.,Piper, P.W.,Pearl, L.H.
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone.
Nat.Struct.Biol., 4:477-482, 1997

PubMed 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.

PubMed: 9187656
DOI: 10.1038/nsb0697-477

Experimental method

X-RAY DIFFRACTION (2.1 Å)