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Journal Article

X-ray structure of a neuronal complexin-SNARE complex from squid


Betz,  H.
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

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Bracher, A., Kadlec, J., Betz, H., & Weissenhorn, W. (2002). X-ray structure of a neuronal complexin-SNARE complex from squid. Journal of Biological Chemistry, 277(29), 26517-26523.

Cite as: http://hdl.handle.net/11858/00-001M-0000-002E-1C25-1
Nerve terminals release neurotransmitters from vesicles into the synaptic cleft upon transient increases in intracellular Ca2+. This exocytotic process requires the formation of trans SNARE complexes and is regulated by accessory proteins including the complexins. Here we report the crystal structure of a squid core complexin-SNARE complex at 2.95-Angstrom resolution. A helical segment of complexin binds in anti- parallel fashion to the four-helix bundle of the core SNARE complex and interacts at its C terminus with syntaxin and synaptobrevin around the ionic zero layer of the SNARE complex. We propose that this structure is part of a multiprotein fusion machinery that regulates vesicle fusion at a late pre-fusion stage. Accordingly, Ca2+ may initiate membrane fusion by acting directly or indirectly on complexin, thus allowing the conformational transitions of the trans SNARE complex that are thought to drive membrane fusion.