NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin

James Hazzard, Thomas C. Südhof, Jose Rizo-Rey

Research output: Contribution to journalArticle

68 Scopus citations

Abstract

Synaptobrevin is a synaptic vesicle protein that has an essential role in exocytosis and forms the SNARE complex with syntaxin and SNAP-25. We have analyzed the structure of isolated synaptobrevin and its binary interaction with syntaxin using NMR spectroscopy. Our results demonstrate that isolated synaptobrevin is largely unfolded in solution. The entire SNARE motif of synaptobrevin is capable of interacting with the isolated C-terminal SNARE motif of syntaxin but only a few residues bind to the full-length cytoplasmic region of syntaxin. This result suggests an interaction between the N- and C-terminal regions of syntaxin that competes with core complex assembly.

Original languageEnglish (US)
Pages (from-to)203-207
Number of pages5
JournalJournal of biomolecular NMR
Volume14
Issue number3
DOIs
StatePublished - Sep 1 1999

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Keywords

  • Exocytosis
  • H, N and C assignments
  • Neurotransmitter release
  • Synaptic protein
  • Synaptobrevin
  • Syntaxin

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy

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