ATOMIC STRUCTURE OF A PRP-FC FUSION PROTEIN

PRP-FC 融合蛋白的原子结构

• 批准号: 7598107
• 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: 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/7598107
• 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.

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。 正常蛋白的修饰形式会引发传染性神经退行性疾病，如牛海绵状脑病(BSE)或人类的克雅氏病(CJD)。Prion蛋白被认为以两种不同的构象存在：“良性的”PrPc形式和具有感染性的“瘙痒形式”PrPsc。了解PrPc的三维结构对于理解向PrPsc的过渡是必不可少的。利用重组PrPc蛋白，核磁共振和X-射线结晶学已经解决了PrPc的C末端，但N末端是非结构化的。在这个方案中，我们将使用一个真核表达的融合蛋白PrP-Fc，通过X射线结晶学来解决PrPc的完整结构。