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Synaptotagmin 1 probably functions as a Ca2+ sensor in neurotransmitter release via its two C2-domains, but no common Ca2+-dependent activity that could underlie a cooperative action between them has been described. The NMR structure of the C2B-domain now reveals a β sandwich that exhibits striking similarities and differences with the C2A-domain. Whereas the bottom face of the C2B-domain has two...
Syntaxin 1A plays a central role in neurotransmitter release through multiple protein–protein interactions. We have used NMR spectroscopy to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure. This 120-residue N-terminal domain is conserved in plasma membrane syntaxins but not in other syntaxins, indicating a specific role in exocytosis...
Synaptotagmin I is a synaptic vesicle protein that is thought to act as a Ca 2+ sensor in neurotransmitter release. The first C 2 domain of synaptotagmin I (C 2 A domain) contains a bipartite Ca 2+ -binding motif and interacts in a Ca 2+ -dependent manner with syntaxin, a central component of the membrane fusion complex. Analysis by nuclear magnetic resonance...
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