CRYO-EM RECONSTRUCTION OF THE HUMAN HSP90:HOP COMPLEX

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 分子伴侣热休克蛋白90(Hsp90)是一个多组分复合体的核心成员，该复合体是包括核受体和细胞周期蛋白在内的许多必需蛋白质的折叠和激活所必需的。对于Hsp90上的‘客户’底物蛋白和辅伴侣蛋白的相互作用，或者在伴侣活性的初始阶段所涉及的结构重排，我们知之甚少。以前的生化研究表明，核受体和其他客户通过Hsp70伴侣蛋白被运送到Hsp90：Hop(Hsp90组织蛋白)复合体。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The molecular chaperone Heat Shock Protein 90 (Hsp90) is the central player in a multi-component complex that is required for the folding and activation of numerous essential proteins including nuclear receptors and cell-cycle kinases. Very little is known about 'client' substrate protein and cochaperone interactions on Hsp90 or the structural rearrangements involved in the initial stages of chaperone activity. Previous biochemical work has shown that nuclear receptors and other clients are delivered to an Hsp90:Hop (Hsp90 organizing protein) complex by the Hsp70 chaperone.