CRYO-EM RECONSTRUCTION OF THE HUMAN HSP90:HOP COMPLEX

人类 HSP90:HOP 复合体的冷冻电镜重建

• 批准号: 8169698
• 负责人: DAVID A. AGARD
• 金额: $ 0.65万
• 依托单位: SCRIPPS RESEARCH INSTITUTE, THE
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169698
• 关键词: Biochemical; Cell Cycle; Client; Complex; Computer Retrieval of Information on Scientific Projects Database; DNA Sequence Rearrangement; Funding; Grant; Heat-Shock Proteins 90; Human; Humulus; Institution; Molecular Chaperones; Nuclear Receptors; Phosphotransferases; Proteins; Receptor Cell; Research; Research Personnel; Resources; Source; Staging; United States National Institutes of Health; Work; protein complex; reconstruction

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.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 中心，不一定是研究者的机构。 分子伴侣热休克蛋白 90 (Hsp90) 是多组分复合物中的核心角色，该复合物是折叠和激活许多必需蛋白质（包括核受体和细胞周期激酶）所必需的。关于“客户”底物蛋白和 Hsp90 上的共伴侣蛋白相互作用或伴侣蛋白活性初始阶段涉及的结构重排知之甚少。先前的生化工作表明，核受体和其他客户由 Hsp70 伴侣传递至 Hsp90:Hop（Hsp90 组织蛋白）复合物。