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

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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.