Ligand-Gated Pentameric ion Channels, from Binding to Gating

Title: Ligand-Gated Pentameric ion Channels, from Binding to Gating

Volume: 2

Author(s): Gabor Maksay

Affiliation:

Keywords: AChBP, pLGIC, nicotinic receptors, GABAA/C receptors, glycine receptors, 5-HT3 receptors, interface binding cavity, binding-gating coupling, allostery, homology modeling

Abstract: X-ray structures of molluscan acetylcholine-binding proteins and procaryotic proton-activated ion channels (ELIC and GLIC) enable us to model the ligand binding and activation mechanism of ligand-gated pentameric ion channels. Common versus distinct features can be deduced from the binding of agonists, antagonists and allosteric modulators in subunit interfaces of nicotinic acetylcholine, A-type γ-aminobutyric acid, glycine and 5-HT3-type serotonin receptors. Ligand interactions in subunit interfaces elicit conformational waves from the closure of the agonist-binding cavity through binding loops, ß-strands and transmembrane helices to pore gating.

Cite this article as:

Maksay Gabor, Ligand-Gated Pentameric ion Channels, from Binding to Gating, Current Molecular Pharmacology 2009; 2 (3) . https://dx.doi.org/10.2174/1874467210902030253