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 language | English (US) |
|---|---|
| Pages (from-to) | 203-207 |
| Number of pages | 5 |
| Journal | Journal of biomolecular NMR |
| Volume | 14 |
| Issue number | 3 |
| DOIs | |
| State | Published - Sep 1 1999 |
Keywords
- Exocytosis
- H, N and C assignments
- Neurotransmitter release
- Synaptic protein
- Synaptobrevin
- Syntaxin
ASJC Scopus subject areas
- Biochemistry
- Spectroscopy
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Hazzard, J., Südhof, T. C., & Rizo-Rey, J. (1999). NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin. Journal of biomolecular NMR, 14(3), 203-207. https://doi.org/10.1023/A:1008382027065