title: [Architecture of receptor-operated ionic channels of biological membranes].
abstract: Ion channels of biological membranes are the key proteins, which provide bioelectric functioning of living systems. These proteins are homo- or heterooligomers assembled from several identical or different subunits. Understanding the architectural organization and functioning of ion channels has been significantly extended due to resolving the crystal structure of several types of voltage-gated and receptor-operated channels. This review summarizes the information obtained from crystal structures of potassium, nicotinic acetylcholine receptor, P2X, and other ligand-gated ion channels. Despite the differences in the function, topology, ionic selectivity, and the subunit stoichiometry, a high similarity in the principles of organization of these macromolecular complexes has been revealed.
authors: P D
authors: PD
authors: Bregestovski
mesh_terms: D000255:Adenosine Triphosphate / Q000502:physiology; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006801:Humans; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry* / Q000502:physiology; D008024:Ligands; D046912:Multiprotein Complexes / Q000737:chemistry / Q000502:physiology; D015221:Potassium Channels / Q000737:chemistry / Q000502:physiology; D011487:Protein Conformation; D018009:Receptors, Glycine / Q000737:chemistry / Q000502:physiology; D017981:Receptors, Neurotransmitter / Q000737:chemistry / Q000502:physiology; D058469:Receptors, Purinergic P2X / Q000737:chemistry / Q000502:physiology
chemical_list: D007473:Ion Channels; D008024:Ligands; D046912:Multiprotein Complexes; D015221:Potassium Channels; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter; D058469:Receptors, Purinergic P2X; D000255:Adenosine Triphosphate