Gloeobacter violaceus ligand-gated ion channel (GLIC) (GLIC)

The Gloeobacter violaceus ligand-gated ion channel (GLIC) is a proton-gated, pentameric ion channel that serves as a prominent prokaryotic model for the Cys-loop receptor family, which includes human nicotinic acetylcholine and GABA_A receptors (Bocquet et al., 2007). Although it originates from a cyanobacterium, GLIC shares high structural homology with human neurotransmitter-gated channels, making it a vital tool for structural biology and pharmacology (Corringer et al., 2012). The protein is particularly noted for its anesthetic binding sites located within the transmembrane domain, where various general anesthetics such as propofol and volatile agents like desflurane exert their effects (Nury et al., 2011). By binding to these sites, anesthetics modulate the channel's gating mechanism, typically stabilizing the open state in GLIC, which contrasts with their inhibitory role in many human homologs (Sauguet et al., 2013). While GLIC itself is not a human therapeutic target, it is indispensable for mapping the molecular interactions of anesthetics and guiding the development of new sedative and anesthetic compounds (Hilf & Dutzler, 2009).

Other names

GLICGloeobacter violaceus proton-gated ion channelGloeobacter ligand-gated ion channelProton-gated ion channel from Gloeobacter violaceus

General anesthetics bind to hydrophobic pockets within the transmembrane domain, specifically the intrasubunit or intersubunit cavities, to allosterically modulate the transition between the closed and open states of the ion channel (Nury et al., 2011; Sauguet et al., 2013).