Pearl L H, Prodromou C
Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, London, SW3 6JB, UK.
Curr Opin Struct Biol. 2000 Feb;10(1):46-51. doi: 10.1016/s0959-440x(99)00047-0.
Until recently, Hsp90 was one of the least well understood of the molecular chaperones, but considerable progress is now being made in unravelling its biochemistry. Hsp90 has now been shown to possess an inherent ATPase that is essential for the activation of authentic 'client' proteins in vivo and in vitro. The molecular detail of Hsp90's interactions with co-chaperones is also becoming clearer and the identification of key roles in assembling regulatory and signalling pathways has made it a target for anticancer drug development. Despite this, a clear understanding of how Hsp90 contributes to the folding and/or activation of its client proteins remains some way off.
直到最近，热休克蛋白90（Hsp90）还是分子伴侣中了解最少的蛋白之一，但目前在阐明其生物化学性质方面正取得相当大的进展。现已表明，Hsp90具有一种内在的ATP酶，这对于体内和体外真正“客户”蛋白的激活至关重要。Hsp90与伴侣蛋白相互作用的分子细节也越来越清晰，并且在组装调节和信号通路中关键作用的确定使其成为抗癌药物开发的靶点。尽管如此，要清楚了解Hsp90如何促进其客户蛋白的折叠和/或激活仍有一段路要走。
