Caplan A J
Dept of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, NY 10029, USA.
Trends Cell Biol. 1999 Jul;9(7):262-8. doi: 10.1016/s0962-8924(99)01580-9.
Hsp90 is a molecular chaperone associated with the folding of signal-transducing proteins, such as steroid hormone receptors and protein kinases. Results from recent studies have shed light on the structure of Hsp90 and have demonstrated that it can bind to and hydrolyse ATP. Hsp90 forms several discrete subcomplexes, each containing distinct groups of co-chaperones that function in folding pathways. Although Hsp90 is not generally involved in the folding of nascent polypeptide chains, there is a growing list of proteins whose activity depends on its function, including heat-shock factor. This review addresses recent developments in our understanding of the structure and function of Hsp90.
热休克蛋白90（Hsp90）是一种分子伴侣，与信号转导蛋白（如类固醇激素受体和蛋白激酶）的折叠相关。近期研究结果揭示了Hsp90的结构，并证明它能够结合并水解ATP。Hsp90形成几个离散的亚复合物，每个亚复合物都包含在折叠途径中发挥作用的不同伴侣蛋白组。虽然Hsp90一般不参与新生多肽链的折叠，但越来越多的蛋白质其活性依赖于Hsp90的功能，包括热休克因子。本综述阐述了我们对Hsp90结构和功能理解的最新进展。
