Three-dimensional structure of the complexin/SNARE complex

Xiaocheng Chen, Diana R Tomchick, Evguenii Kovrigin, Demet Araç, Mischa Machius, Thomas C. Südhof, Jose Rizo-Rey

Research output: Contribution to journalArticle

291 Scopus citations

Abstract

During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca2+-evoked neurotransmitter release. A combined X-ray and TROSY-based NMR study now reveals the atomic structure of the complexin/SNARE complex. Complexin binds in an antiparallel α-helical conformation to the groove between the synaptobrevin and syntaxin helices. This interaction stabilizes the interface between these two helices, which bears the repulsive forces between the apposed membranes. These results suggest that complexin stabilizes the fully assembled SNARE complex as a key step that enables the exquisitely high speed of Ca2+-evoked neurotransmitter release.

Original languageEnglish (US)
Pages (from-to)397-409
Number of pages13
JournalNeuron
Volume33
Issue number3
DOIs
StatePublished - Jan 31 2002

ASJC Scopus subject areas

  • Neuroscience(all)

Fingerprint Dive into the research topics of 'Three-dimensional structure of the complexin/SNARE complex'. Together they form a unique fingerprint.

  • Cite this