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![Three different views of the high resolution structure of a truncated neuronal SNARE complex. Legend: synaptobrevin-2 (red), Syntaxin-1 (violet), SNAP-25 (purple). [1]](http://www.jgames.co.uk/title/Image:Coresnarecomplex.png)
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Structure
Out of four α-helices of the core SNARE complex one is contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 (in neurons).
Function
SNARE proteins are the key components of the molecular machinery that drives fusion of membranes in exocytosis. Their function however is subject to fine tuning by various regulatory protein collectively referred to as SNARE masters.
Classification
Because all proteins belonging to VAMP/synaptobrevin family share common structural feature, they have been classified as R-SNAREs. An alternative classification (v- and t-SNAREs) exists that takes into account origin of synaptobrevin-bearing organelle rather than their structural properties.
Clinical significance
Synaptobrevin is degraded by Tetanospasmin, a protein derived from Clostridium tetani.
References and notes
- ^ Baumert M, Maycox PR, Navone F, De Camilli P, Jahn R (1989). "Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain". EMBO J 8: 379–384. PMID 2498078.
- ^ Bock JB, Scheller RH (1999). "SNARE proteins mediate lipid bilayer fusion". PNAS 96: 12227–12229. doi:. PMID 10535902.
- ^ Ernst JA, Brunger AT (2003). "High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex". J Biol Chem 278: 8630–8636. doi:. PMID 12496247.
- ^ Fasshauer D, Sutton RB, Brunger AT, Jahn R (1998). "Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs". PNAS 95: 15781–15786. doi:. PMID 9861047.
- ^ Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Sollner TH, Rothman JE (1998). "SNAREpins: minimal machinery for membrane fusion". Cell 92: 759–772. doi:.
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