Journal of Biomolecular NMR

, Volume 14, Issue 3, pp 203–207

NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin

  • James Hazzard
  • Thomas C. Südhof
  • Josep Rizo
Article

DOI: 10.1023/A:1008382027065

Cite this article as:
Hazzard, J., Südhof, T.C. & Rizo, J. J Biomol NMR (1999) 14: 203. doi:10.1023/A:1008382027065

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.

exocytosis 115N and 13C assignments neurotransmitter release synaptic protein synaptobrevin syntaxin 

Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • James Hazzard
    • 1
  • Thomas C. Südhof
    • 2
  • Josep Rizo
    • 1
  1. 1.Departments of Biochemistry and PharmacologyThe University of Texas Southwestern Medical CenterDallasU.S.A.
  2. 2.Department of Molecular Genetics and Howard Hughes Medical InstituteThe University of Texas Southwestern Medical CenterDallasU.S.A.

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