STRUCTURAL BASIS OF HUMAN PACSIN 1

人类 PACSIN 1 的结构基础

• 批准号: 7957303
• 负责人: QI WANG
• 金额: $ 2.05万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-07-01 至 2010-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7957303
• 关键词: Binding; C-terminal; Capsid Proteins; Cells; Computer Retrieval of Information on Scientific Projects Database; Crystallography; Data Set; Dynamin; Endocytosis; Event; Funding; Grant; Institution; Light; Membrane; Modeling; N-terminal; Neurons; Play; Proteins; Qualifying; Regulation; Research; Research Personnel; Resolution; Resources; Role; SH3 Domains; Source; Structure; Surface; Synaptic Vesicles; Synchrotrons; Testing; Transportation; United States National Institutes of Health; Vesicle; base; computerized data processing; protein structure; self assembly

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. PACSIN 1 is a neuron specific protein that plays a center role in synaptic vesicle endocytosis of neuron cells. PACSIN I contains two well-defined domains. The N-terminal F-BAR domain has been shown to play an important role in vesicle formation and related membrane remodeling events. Low resolution TEM study indicates the F-BAR domain can self-assembly and form a protein coat on the membrane surface and constrain its geometry. The C-terminal SH3 domain can bind with NWASP and Dynamin, which are key proteins involved in vesicle formation and the transportation. Our research is trying to use the crystallographic study to understand its function and regulation at the atomic level. The obtained crystal structures will serve as the first high-resolution models to investigate its membrane binding, regulation and activation mechanisms. The onsite activities will be including 1) screen and test crystals quality; 2) Collect datasets on good quality crystals and process the data 3) Solve the protein structures based on qualified datasets.

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。 PACSIN 1 是一种神经元特异性蛋白，在神经元细胞的突触小泡内吞作用中发挥核心作用。 PACSIN I 包含两个明确定义的域。 N 末端 F-BAR 结构域已被证明在囊泡形成和相关膜重塑事件中发挥重要作用。低分辨率 TEM 研究表明 F-BAR 结构域可以自组装并在膜表面形成蛋白质涂层并限制其几何形状。 C 端 SH3 结构域可以与 NWASP 和 Dynamin 结合，它们是参与囊泡形成和运输的关键蛋白。我们的研究试图利用晶体学研究来了解其在原子水平上的功能和调控。获得的晶体结构将作为第一个高分辨率模型来研究其膜结合、调节和激活机制。现场活动将包括1）筛选和测试晶体质量； 2) 收集优质晶体的数据集并处理数据 3) 根据合格的数据集解析蛋白质结构。