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Several ion channel structures have recently been determined, including MthK (a bacterial K+ channel in an open state), KirBac (a bacterial homolog of mammalian inward rectifier K+ channels), KvAP (a bacterial voltage-activated K+ channel) and the pore domain of the nicotinic acetylcholine receptor. Analysis of these structures has increased our understanding of the molecular mechanisms underlying channel gating. A hydrophobic gate appears to operate in a number of channels. Structures of ligand binding domains provide some clues as to how ligand-induced conformational changes control channel gating, but further experimental and computational studies are required before a full picture emerges.


Journal article


Curr Opin Drug Discov Devel

Publication Date





611 - 619


Animals, Bacterial Proteins, Ion Channel Gating, Ion Channels, Ligands, Membrane Proteins, Protein Structure, Quaternary, Protein Structure, Tertiary, Viral Matrix Proteins