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。 突触素是一种囊泡相关蛋白，含有两个同源的C2结构域(C2a和C2b)。这些结构域在神经元中介导钙依赖的胞吐作用。有相当多的间接证据表明，在胞吐过程中，生理性多聚体是突触素活性的一部分；然而，还没有直接的证据。利用SSRL获得的更高分辨率的X射线数据，这种人类突触素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，这项实验将代表第一个自相关的突触素分子，它可能是突触素1完整功能域的最高分辨率结构。分析每个突触素分子的相对灵活性将有助于更准确地描述神经元中的突触素功能。

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.