STRUCTURAL BASIS OF CELL MEMBRANE TARGETING, ADHESION, AND SIGNALING

细胞膜靶向、粘附和信号传导的结构基础

• 批准号: 8170160
• 负责人: William I Weis
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 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 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170160
• 关键词: Actins; Adhesions; Allosteric Regulation; Binding; Cadherins; Cell Adhesion; Cell membrane; Complex; Computer Retrieval of Information on Scientific Projects Database; Couples; Cytoskeleton; F-actin-binding proteins; Funding; Grant; Institution; Length; Regulation; Research; Research Personnel; Resources; SNAP receptor; Signal Transduction; Source; Specificity; Structure; United States National Institutes of Health; base; mutant; programs; protein structure; synchrotron radiation; syntaxin

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. This program aims to determine the structures of proteins involved in cell membrane targeting, adhesion, and signaling, in order to establish the mechanism and specificity of their interactions. There are currently two projects with crystals that require synchrotron radiation. 1. Structure of full-length a-catenin, an F-actin binding protein that couples cadherin-based cell adhesion to regulation of the actin cytoskeleton. 2. Complexes of the SNARE regulator Munc18a bound to mutants of the SNARE syntaxin that will allow understanding of allosteric regulation of this interaction.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 该计划旨在确定参与细胞膜靶向，粘附和信号传导的蛋白质的结构，以建立它们相互作用的机制和特异性。 目前有两个项目的晶体需要同步辐射。 1.全长α-连环蛋白的结构，它是一种F-肌动蛋白结合蛋白，将钙粘蛋白基细胞粘附与肌动蛋白细胞骨架的调节偶联。2. SNARE调节因子Munc 18 a的复合物与SNARE突触融合蛋白的突变体结合，这将有助于了解这种相互作用的变构调节。