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

Imma Fernandez, Josep Ubach, Irina Dulubova, Xiangyang Zhang, Thomas C. Südhof, Jose Rizo-Rey

Research output: Contribution to journalArticle

238 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)841-849
Number of pages9
JournalCell
Volume94
Issue number6
DOIs
StatePublished - Sep 18 1998

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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