热休克蛋白90，一种用于折叠和调节的伴侣蛋白。
Heat-shock protein 90, a chaperone for folding and regulation.
作者信息
Picard D
出版信息
Cell Mol Life Sci. 2002 Oct;59(10):1640-8. doi: 10.1007/pl00012491.
Abstract
Heat-shock protein 90 (Hsp90) is an abundant and highly conserved molecular chaperone that is essential for viability in eukaryotes. Hsp90 fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins. A remarkable proportion of its substrates are proteins involved in cell cycle control and signal transduction. Hsp90 acts with a cohort of Hsp90 co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. The large conformational flexibility of Hsp90 and a multitude of dynamic co-chaperone complexes contribute to generating functional diversity, and allow Hsp90 to assist a wide range of substrates.
摘要
热休克蛋白90（Hsp90）是一种丰富且高度保守的分子伴侣，对真核生物的生存至关重要。Hsp90在促进细胞溶质蛋白的折叠、维持结构完整性以及适当调节方面发挥着管家功能。其相当一部分底物是参与细胞周期调控和信号转导的蛋白质。Hsp90与一群Hsp90共伴侣蛋白共同作用，这些共伴侣蛋白调节其底物识别、ATP酶循环和伴侣功能。Hsp90的大构象灵活性和众多动态共伴侣复合物有助于产生功能多样性，并使Hsp90能够协助多种底物。
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