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 - 1999 |
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Keywords
- H, N and C assignments
- Exocytosis
- Neurotransmitter release
- Synaptic protein
- Synaptobrevin
- Syntaxin
ASJC Scopus subject areas
- Spectroscopy
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
Cite this
NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin. / Hazzard, James; Südhof, Thomas C.; Rizo-Rey, Jose.
In: Journal of Biomolecular NMR, Vol. 14, No. 3, 1999, p. 203-207.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin
AU - Hazzard, James
AU - Südhof, Thomas C.
AU - Rizo-Rey, Jose
PY - 1999
Y1 - 1999
N2 - 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.
AB - 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.
KW - H, N and C assignments
KW - Exocytosis
KW - Neurotransmitter release
KW - Synaptic protein
KW - Synaptobrevin
KW - Syntaxin
UR - http://www.scopus.com/inward/record.url?scp=0344289516&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0344289516&partnerID=8YFLogxK
U2 - 10.1023/A:1008382027065
DO - 10.1023/A:1008382027065
M3 - Article
C2 - 10481273
AN - SCOPUS:0344289516
VL - 14
SP - 203
EP - 207
JO - Journal of Biomolecular NMR
JF - Journal of Biomolecular NMR
SN - 0925-2738
IS - 3
ER -