Prodromou C, Roe S M, Piper P W, Pearl L H
Department of Biochemistry and Molecular Biology, University College London, UK.
Nat Struct Biol. 1997 Jun;4(6):477-82. doi: 10.1038/nsb0697-477.
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.
热休克蛋白90（Hsp90）是许多信号转导蛋白的高度特异性伴侣蛋白，包括类固醇激素受体和多种蛋白激酶。酵母Hsp90 N端结构域的晶体结构揭示了一种基于高度扭曲的16股β折叠的二聚体结构，其拓扑结构表明完整的Hsp90二聚体可能存在30个结构域交换的结构。二聚体中β折叠的相对面定义了一个潜在的肽结合裂隙，这表明N结构域可能在配体蛋白与Hsp90的结合中充当分子“夹子”。
