NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin
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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.
- NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin
Journal of Biomolecular NMR
Volume 14, Issue 3 , pp 203-207
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- Kluwer Academic Publishers
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- 15N and 13C assignments
- neurotransmitter release
- synaptic protein
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- Author Affiliations
- 1. Departments of Biochemistry and Pharmacology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX, 75235, U.S.A.
- 2. Department of Molecular Genetics and Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX, 75235, U.S.A.