NMR analysis of the structure of synaptobrevin and of its interaction withsyntaxin

Citation
J. Hazzard et al., NMR analysis of the structure of synaptobrevin and of its interaction withsyntaxin, J BIOM NMR, 14(3), 1999, pp. 203-207
Citations number
17
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOMOLECULAR NMR
ISSN journal
09252738 → ACNP
Volume
14
Issue
3
Year of publication
1999
Pages
203 - 207
Database
ISI
SICI code
0925-2738(199907)14:3<203:NAOTSO>2.0.ZU;2-Y
Abstract
Synaptobrevin is a synaptic vesicle protein that has an essential role in e xocytosis and forms the SNARE complex with syntaxin and SNAP-25. We have an alyzed the structure of isolated synaptobrevin and its binary interaction w ith syntaxin using NMR spectroscopy. Our results demonstrate that isolated synaptobrevin is largely unfolded in solution. The entire SNARE motif of sy naptobrevin is capable of interacting with the isolated C-terminal SNARE mo tif 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.