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Cell. 1998 Sep 18;94(6):841-9.

Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.

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1
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235, USA.

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.

PMID:
9753330
[Indexed for MEDLINE]
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