Ligand-gated pentameric ion channels, from binding to gating.
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 gamma-aminobutyric acid, glycine and 5-HT(3)-type serotonin receptors. Ligand interactions in subunit interfaces elicit conformational waves from the closure of the agonist-binding cavity through binding loops, beta-strands and transmembrane helices to pore gating.
Maksay
Gábor
G
Department of Molecular Pharmacology, Institute of Biomolecular Chemistry, Chemical Research Center, Hungarian Academy of Sciences, Budapest, Hungary. maksay@chemres.hu
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology*; D007473:Ion Channels / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D008969:Molecular Sequence Data; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D017981:Receptors, Neurotransmitter / Q000819:agonists / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D016415:Sequence Alignment
D007473:Ion Channels; D008024:Ligands; D021122:Protein Subunits; D017981:Receptors, Neurotransmitter