ATOMIC STRUCTURE OF A PRP-FC FUSION PROTEIN

PRP-FC 融合蛋白的原子结构

• 批准号: 7721881
• 负责人: QIANG ZHANG
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721881
• 关键词: Benign; Bovine Spongiform Encephalopathy; Chimeric Proteins; Computer Retrieval of Information on Scientific Projects Database; Creutzfeldt-Jakob Syndrome; Crystallography; Funding; Grant; Human; Institution; Knowledge; Molecular Conformation; Neurodegenerative Disorders; Prions; Protein C; Recombinants; Research; Research Personnel; Resources; Scrapie; Source; Structure; Thinking; United States National Institutes of Health; three dimensional structure

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. A modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in humans. Prion proteins are thought to exist in two different conformations: the 'benign' PrPc form, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential for understanding the transition to PrPsc. Using recombinant prion proteins, the C terminus of PrPc has been solved by NMR and x-ray crystallography, but the N terminus was found to be unstructured. In this proposal, we will employ an eukaryotically expressed fusion protein, PrP-Fc, to solve the complete structure of PrPc through x-ray crystallography.

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 对于中心来说，它不一定是研究者的机构。 正常朊病毒蛋白的修饰形式会引发传染性神经退行性疾病，例如牛海绵状脑病（BSE）或人类克雅氏病（CJD）。朊病毒蛋白被认为以两种不同的构象存在：“良性”PrPc 形式和传染性“痒病形式”PrPsc。了解 PrPc 的三维结构对于理解 PrPsc 的转变至关重要。使用重组朊病毒蛋白，PrPc 的 C 末端已通过 NMR 和 X 射线晶体学解析，但发现 N 末端是非结构化的。在本提案中，我们将采用真核表达的融合蛋白PrP-Fc，通过X射线晶体学解析PrPc的完整结构。