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Structural titration of receptor ion channel GLIC gating by HS-AFM

Abstract : Gloeobacter violaceus ligand-gated ion channel (GLIC), a proton-gated, cation-selective channel, is a prokaryotic homolog of the pentameric Cys-loop receptor ligand-gated ion channel family. Despite large changes in ion conductance, small conformational changes were detected in X-ray structures of detergent-solubilized GLIC at pH 4 (active/desensitized state) and pH 7 (closed state). Here, we used high-speed atomic force microscopy (HS-AFM) combined with a buffer exchange system to perform structural titration experiments to visualize GLIC gating at the single-molecule level under native conditions. Reference-free 2D classification revealed channels in multiple conformational states during pH gating. We find changes of protein-protein interactions so far elusive and conformational dynamics much larger than previously assumed. Asymmetric pentamers populate early stages of activation, which provides evidence for an intermediate preactivated state.
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Contributor : Pierre-Jean Corringer <>
Submitted on : Tuesday, December 3, 2019 - 9:56:48 AM
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Yi Ruan, Kevin Kao, Solène Lefebvre, Arin Marchesi, Pierre-Jean Corringer, et al.. Structural titration of receptor ion channel GLIC gating by HS-AFM. Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2018, 115 (41), pp.10333-10338. ⟨10.1073/pnas.1805621115⟩. ⟨pasteur-02390441⟩



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