Abstract

Ligand-gated ion channels are critical mediators of electrochemical signal transduction across evolution. Biophysical and pharmacological development in this family relies on high-quality structural data in multiple, subtly distinct functional states; however, structural data remain limited, particularly for the native closed state. Here, we report cryo-electron microscopy structures of the proton-gated Gloeobacter violaceus ligand-gated ion channel (GLIC) under resting and activating conditions (pH 7, 5, and 3).

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