Ion channel structures: a review of recent progress.
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.
University of Oxford, Laboratory of Molecular Biophysics, Department of Biochemistry, South Parks Road, Oxford, OX1 3QU, UK.
Carmen
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Domene
Shozeb
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Haider
Mark S P
MS
Sansom
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry*; D008024:Ligands; D008565:Membrane Proteins / Q000737:chemistry; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D014763:Viral Matrix Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D007473:Ion Channels; D008024:Ligands; C031540:M-protein, influenza virus; D008565:Membrane Proteins; D014763:Viral Matrix Proteins