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.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 HSP70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。该蛋白质为70 kDa，但具有三域结构：ATPase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）。伴侣结合了展开的蛋白质，并通过变构机制与ATP结合，将其对这些底物的亲和力切换。可以单独表达和折叠的域以及构造构造两个域。我们已经在底物结合结构域（核苷酸结合结构域）上发表了结构，并最近定义了包含两个域的54 kDa构建体的全局结构。当前的实验用NOE定义了域之间的接口部分。蛋白质为13C，15N，2H和13C1H3。