Cell
Volume 94, Issue 6, 18 September 1998, Pages 841-849
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Article
Three-Dimensional Structure of an Evolutionarily Conserved N-Terminal Domain of Syntaxin 1A

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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 α 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.

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