Abstract
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. The domain contains three long alpha helices that form an up-and-down bundle with a left-handed twist. A striking residue conservation is observed throughout a long groove that is likely to provide a specific surface for protein-protein interactions. A highly acidic region binds to the C2A domain of synaptotagmin I in a Ca2+-dependent interaction that may serve as an electrostatic switch in neurotransmitter release.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antigens, Surface / chemistry*
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Antigens, Surface / genetics*
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Antigens, Surface / metabolism
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Calcium / metabolism
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Calcium-Binding Proteins / metabolism
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Evolution, Molecular*
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Magnetic Resonance Spectroscopy
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Membrane Glycoproteins / metabolism
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / genetics*
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Nerve Tissue Proteins / metabolism
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Neurotransmitter Agents / metabolism
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Protein Binding / physiology
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Rats
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Sequence Homology, Amino Acid
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Synaptic Transmission / physiology
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Synaptotagmin I
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Synaptotagmins
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Syntaxin 1
Substances
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Antigens, Surface
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Calcium-Binding Proteins
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Membrane Glycoproteins
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Nerve Tissue Proteins
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Neurotransmitter Agents
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Stx1a protein, rat
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Synaptotagmin I
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Syntaxin 1
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Syt1 protein, rat
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Synaptotagmins
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Calcium