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  • Title: A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone.
    Author: Prodromou C, Roe SM, Piper PW, Pearl LH.
    Journal: Nat Struct Biol; 1997 Jun; 4(6):477-82. PubMed ID: 9187656.
    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.
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