3D STRUCTURE DNAK-TTH

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。 HSP70蛋白在所有已知的细胞结构中介导蛋白质的运输、折叠和重折叠。该蛋白全长70 kDa，具有三个结构域：ATPase结构域(44 KDa)、底物结合区(15-20 kDa)和C-末端结构域(15-20 kDa)。伴侣与未折叠的蛋白质结合，并通过变构机制与ATP结合来切换其对这些底物的亲和力。结构域以及包含这两个结构域的构建体可以单独表达和折叠。我们已经公布了底物结合域、核苷酸结合域的结构，最近还定义了包含这两个结构域的54 kDa结构的全球结构。目前的实验用于定义结构域之间的界面部分，与NOE的。该蛋白是13C，15N，2H和13C1H3标记的。

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. Hsp70 proteins mediate trafficking, folding and refolding of proteins in all known cellular structures. The protein is 70 kDa, but has a three-domain structure: ATPase domain (44 kDa) substrate-binding domain (15-20 kDa) and C-terminal domain (15-20 kDa). The chaperone binds to unfolded proteins and switches its affinity for these substrates by binding to ATP through an allosteric mechanism. The domains as well as constructs containg both domains can be individually expressed and folded. We have published structures on the substrate binding domain, the nucleotide binding domain, and have recently defined a global structure for a 54 kDa construct containing both domains. The current experiments serve to define the interface section between the domains, with NOE's. The protein is 13C, 15N, 2H and 13C1H3 labeled.