Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Three-dimensional structure of the complexin/SNARE complex.

Xiaocheng Chen1, Diana R Tomchick, Evguenii Kovrigin

  • 1Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Neuron
|February 8, 2002
PubMed
Summary

Complexin protein stabilizes the SNARE complex, a crucial step for rapid calcium-evoked neurotransmitter release. This structural insight explains the speed of essential neuronal communication.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Guiding AlphaFold to predict how Munc13-1 opens Syntaxin-1.

FEBS open bio·2026
Same author

TIR-like NADases act in bacterial immunity and the RNA vault.

bioRxiv : the preprint server for biology·2026
Same author

Reciprocal repulsions enforce heterotypic dendrite segregation in an olfactory circuit.

bioRxiv : the preprint server for biology·2026
Same author

Adhesion G protein-coupled receptors.

Pharmacological reviews·2026
Same author

Efficient In Vivo Pharmacological Inhibition of ΔFOSB, an AP-1 Transcription Factor, in the Brain.

ACS chemical neuroscience·2026
Same author

The local detergent model of SNARE-mediated membrane fusion.

Journal of cell science·2026

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Structural Biology

Background:

  • Neuronal SNARE proteins (synaptobrevin/VAMP, syntaxin, SNAP-25) form a complex essential for neurotransmitter release.
  • Complexin is vital for efficient calcium-evoked neurotransmitter release, but its precise role is unclear.

Purpose of the Study:

  • To elucidate the atomic structure of the complexin/SNARE complex.
  • To understand how complexin binding influences SNARE complex function and membrane fusion.

Main Methods:

  • Combined X-ray crystallography and Transverse Relaxation-Optimized Spectroscopy (TROSY)-based Nuclear Magnetic Resonance (NMR) studies.
  • Structural analysis of the complexin/SNARE protein interaction.

Main Results:

Related Experiment Videos

  • The atomic structure reveals complexin binds in an antiparallel alpha-helical conformation within the groove of the SNARE complex.
  • Complexin binding stabilizes the interface between synaptobrevin and syntaxin helices, counteracting repulsive forces between membranes.
  • This stabilization is proposed as a key mechanism enabling rapid calcium-evoked neurotransmitter release.

Conclusions:

  • Complexin acts as a crucial stabilizer of the assembled SNARE complex.
  • The structural insights provided explain the high speed of calcium-evoked neurotransmitter release.
  • This finding deepens our understanding of the molecular mechanisms underlying synaptic transmission.