3D STRUCTURE DNAK-TTH

3D 结构 DNAK-TTH

• 批准号: 7598808
• 负责人: ERIK R ZUIDERWEG
• 金额: $ 0.07万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7598808
• 关键词: ATPase Domain; Affinity; Binding; C-terminal; Cellular Structures; Computer Retrieval of Information on Scientific Projects Database; Funding; Grant; Institution; Label; Mediating; Molecular Chaperones; Nucleotides; Proteins; Publishing; Research; Research Personnel; Resources; Source; Structure; United States National Institutes of Health; research study; three dimensional structure; trafficking

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.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 Hsp 70蛋白介导所有已知细胞结构中蛋白质的运输、折叠和重折叠。该蛋白分子量为70 kDa，但具有三个结构域：ATP酶结构域（44 kDa）、底物结合结构域（15-20 kDa）和C-末端结构域（15-20 kDa）。分子伴侣结合未折叠的蛋白质，并通过变构机制与ATP结合来改变其对这些底物的亲和力。所述结构域以及含有两个结构域的构建体可以单独表达和折叠。我们已经发表了结构上的底物结合域，核苷酸结合域，并在最近定义了一个全球性的结构为54 kDa的构建体含有这两个域。目前的实验用于定义域之间的界面部分，与NOE的。蛋白质被13 C、15 N、2 H和13 C1 H3标记。