STRUCTURAL STUDIES OF BRCT RECOGNITION OF PHOSPHOPROTEINS

BRCT 磷酸蛋白识别的结构研究

• 批准号: 7721202
• 负责人: NIKOLA P PAVLETICH
• 金额: $ 0.97万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-05-15 至 2009-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721202
• 关键词: Binding; Computer Retrieval of Information on Scientific Projects Database; Funding; Grant; Institution; Pathway interactions; Phosphoproteins; Physiological; Proteins; Research; Research Personnel; Resources; Single-Stranded DNA; Source; Structure; United States National Institutes of Health; homologous recombination

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. Brca2 is believed to be a critical component in homologous recombination pathway. We have shown how th c-terminal of Brca2 binds with single strand DNA. In order to understand its physiological function, we would like to determine structure of Brca2 protein with its recognized substrate and interacting partners, including rad51.

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。 Brca2被认为是同源重组途径中的关键组成部分。我们已经展示了 Brca2 的 C 末端如何与单链 DNA 结合。为了了解其生理功能，我们希望确定 Brca2 蛋白及其识别底物和相互作用伙伴（包括 rad51）的结构。