CRYSTAL STRUCTURE OF THE C2A-C2B DOMAINS OF HUMAN SYNAPTOTAGMIN 1

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。 突触结合蛋白是一种囊泡相关蛋白，含有两个同源的C2结构域（C2 A和C2B）。这些结构域介导神经元中的Ca+2依赖性胞吐作用。有相当数量的间接证据表明，在胞吐过程中，生理多聚体是突触结合蛋白活性的一部分;然而，没有直接的证据被假定。随着SSRL获得的更高分辨率的X射线数据，这种人类突触结合蛋白1的晶体形式应该有助于解释这种多聚体的结构起源。此外，该实验将代表自缔合的突触结合蛋白分子的第一个实例，并且它可能是突触结合蛋白1的完整功能结构域的最高分辨率结构。对突触结合蛋白每种分子的相对灵活性的分析将有助于更准确地描述突触结合蛋白在神经元中的功能。

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. Synaptotagmin is a vesicle-associated protein containing two homologous C2 domains (C2A and C2B). These domains mediate Ca+2-dependent exocytosis in neurons. There has been a considerable amount of indirect evidence implicating a physiological multimer as a part of synaptotagmin's activity during the process of exocytosis; however, no direct evidence has been posited. With the higher resolution x-ray data obtainable at SSRL, this crystal form of human synaptotagmin 1 should help explain the structural origins of this multimer. Also, this experiment will represent the first instance of a synaptotagmin molecule that self-associates, and it could be the highest resolution structure of the complete functional domains of synaptotagmin 1. Analysis of the relative flexibility of each molecule of synaptotagmin will contribute to a more accurate description of synaptotagmin function in the neuron.