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

65 Citations (Scopus)

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 - 1999

Fingerprint

R-SNARE Proteins
Qa-SNARE Proteins
SNARE Proteins
Nuclear magnetic resonance
Synaptic Vesicles
Exocytosis
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Proteins

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 journalArticle

@article{6686dc8248e24488940a7c102df664a5,
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 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.",
keywords = "H, N and C assignments, Exocytosis, Neurotransmitter release, Synaptic protein, Synaptobrevin, Syntaxin",
author = "James Hazzard and S{\"u}dhof, {Thomas C.} and Jose Rizo-Rey",
year = "1999",
doi = "10.1023/A:1008382027065",
language = "English (US)",
volume = "14",
pages = "203--207",
journal = "Journal of Biomolecular NMR",
issn = "0925-2738",
publisher = "Springer Netherlands",
number = "3",

}

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 -