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

CLC chloride channels: correlating structure with function.

Raúl Estévez1, Thomas J Jentsch

  • 1Zentrum für Molekulare Neurobiologie, Universität Hamburg, Falkenried 94, Germany.

Current Opinion in Structural Biology
|August 7, 2002
PubMed
Summary

Crystal structures reveal CLC chloride channels have a complex

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

Mechanistic insights into DCPIB inhibition of VRAC: Electrostatic control and binding plasticity.

The Journal of general physiology·2026
Same author

Structural insights into a conserved mechanism of choline translocation through CHT.

Science advances·2026
Same author

L-Ergothioneine Attenuates Nephrolithiasis by Modulating Redox Signaling and Mitochondrial Function in Cystine and Calcium Oxalate Models.

Antioxidants & redox signaling·2026
Same author

LRRC8-Mediated Glutamate Release from Astrocytes Is Not Increased During the Initiation of Experimental Temporal Lobe Epilepsy.

International journal of molecular sciences·2026
Same author

Metabolic acidosis causes a Fanconi-like syndrome with intracellular trafficking defects and proximal tubule dysfunction.

Science translational medicine·2026
Same author

A protective cGAMP-mediated anti-tumor immune response can proceed without LRRC8/VRAC channels.

The Journal of biological chemistry·2025

Area of Science:

  • Molecular biology
  • Structural biology
  • Biophysics

Background:

  • Chloride channels (CLCs) are crucial membrane proteins found across diverse life forms.
  • Previous studies suggested CLC channels form homodimers with a 'double-barrelled' pore structure.
  • Understanding CLC channel gating and permeation mechanisms is vital.

Purpose of the Study:

  • To elucidate the detailed structure of bacterial CLC proteins.
  • To confirm and refine previous functional hypotheses about CLC channels.
  • To provide a structural basis for interpreting mutagenesis and electrophysiology data.

Main Methods:

  • X-ray diffraction analysis of two bacterial CLC proteins.
  • Analysis of protein crystal structures.

Main Results:

  • Confirmed the homodimeric, 'double-barrelled' architecture of CLC channels.
  • Revealed an unprecedented and complex channel structure at atomic resolution.
  • Identified specific interactions of chloride ions with pore-lining helices and a gating glutamate residue.

Conclusions:

  • The crystal structures validate previous functional studies on CLC channels.
  • The detailed structure provides a framework for understanding CLC channel gating and ion permeation.
  • This work offers new insights into the molecular mechanisms of CLC channel function.

Related Experiment Videos