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: 8362199
• 负责人: William I Weis
• 金额: $ 0.06万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362199
• 关键词: Actins; Adhesions; Allosteric Regulation; Binding; Cadherins; Cell Adhesion; Cell membrane; Complex; Couples; Cytoskeleton; F-actin-binding proteins; Funding; Grant; Length; National Center for Research Resources; Principal Investigator; Radiation; Regulation; Research; Research Infrastructure; Resources; SNAP receptor; Signal Transduction; Source; Specificity; Structure; United States National Institutes of Health; base; cost; mutant; programs; protein structure; structural biology; synchrotron radiation; syntaxin

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 该项目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。 目前有两个晶体项目需要同步辐射。 1. 全长α-连环蛋白的结构，这是一种 F-肌动蛋白结合蛋白，可将基于钙粘蛋白的细胞粘附与肌动蛋白细胞骨架的调节结合起来。 2. SNARE 调节因子 Munc18a 的复合物与 SNARE 突触蛋白突变体结合，这将有助于理解这种相互作用的变构调节。