Conformational transitions underlying pore opening and desensitization in membrane-embedded gloeobacter violaceus ligand-gated ion channel (GLIC)

Abstract

Background: GLIC, a prokaryotic homologue of pentameric ligand-gated ion channels (LGIC), is activated by protons, and crystal structures suggest a putative open conformation. Results: EPR-spectroscopic studies in the pore-lining segment reveals major conformational changes during activation and desensitization. Conclusion: Gating mechanism in GLIC involves distinct activation and desensitization gates. Significance: These studies provide insights into the role of structural dynamics in the functioning of LGIC. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.