STRUCTURAL BASIS OF CELL MEMBRANE TARGETING, ADHESION, AND SIGNALING

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。 该计划旨在确定参与细胞膜靶向、黏附和信号传递的蛋白质的结构，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，这是一种F-肌动蛋白结合蛋白，它将基于钙粘附素的细胞黏附与肌动蛋白细胞骨架的调节结合在一起。2.SNARE调节剂Munc18a的复合体与SNARE合成素的突变体结合，这将允许理解这种相互作用的变构调节。

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.