Erwinia chrysanthemi ligand-gated ion channel (ELIC)

The Erwinia chrysanthemi ligand-gated ion channel (ELIC) is a bacterial homolog of the Cys-loop family of ligand-gated ion channels[2][5][8][9]. ELIC forms a pentameric structure that is closely related in architecture to human nicotinic acetylcholine, GABA, and glycine receptors[3][6][5][8]. It is activated by small primary amines, such as GABA, but with much lower potency than its eukaryotic counterparts, requiring high micromolar to millimolar concentrations for activation[1][2][5][9]. Quaternary amines (e.g., acetylcholine) act as competitive antagonists but do not activate the channel[9].\n\nELIC's functional properties as a cation-selective channel make it an important experimental model for understanding the structure, gating, and ligand-recognition mechanisms of the Cys-loop receptor superfamily[5][8][9]. High-resolution structural studies—including cryo-EM and X-ray crystallography—have elucidated its channel opening, agonist binding, lipid and phospholipid modulation, and conformational changes[6][7][8][9]. ELIC retains its functional characteristics when expressed in bacterial membranes and is modulated by membrane lipids, such as phosphatidylglycerol and cardiolipin[3][7][8]. It is not directly relevant as a target for drugs or human disease but underpins research that informs therapeutic design and mechanistic study in higher organisms.\n\nELIC is not a misspelling or ambiguous term; however, while it functions as an ion channel and shares homology with therapeutic targets in humans, it itself is not a therapeutic target for any approved or investigational drugs—its value lies in its role as a structural and mechanistic analog.

Other names

Erwinia ligand-gated ion channelELIC

Ligand binding to the extracellular domain induces conformational changes, opening a cation-selective channel\nActivated by small amines; not by quaternary amines (e.g., acetylcholine)\nInhibited by acetylcholine (competitive antagonist)