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pubmed-article:9187656pubmed:abstractTextHsp90 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.lld:pubmed
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pubmed-article:9187656pubmed:articleTitleA molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone.lld:pubmed
pubmed-article:9187656pubmed:affiliationDepartment of Biochemistry and Molecular Biology, University College London, UK.lld:pubmed
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