title: NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin.
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 in 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.
authors.affiliation: Department of Biochemistry, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235, USA.
authors.forename: J
authors.initials: J
authors.lastname: Hazzard
authors.forename: T C
authors.initials: TC
authors.lastname: Südhof
authors.forename: J
authors.initials: J
authors.lastname: Rizo
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D011994:Recombinant Proteins