Journal
JOURNAL OF NEUROCHEMISTRY
Volume 88, Issue 4, Pages 782-799Publisher
WILEY
DOI: 10.1111/j.1471-4159.2004.02261.x
Keywords
channel agonists; glutamate-gated ion channels; ligand-receptor interactions; open channel block; voltage-gated ion channels
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In the last decade, the idea of common organization of certain ion channel families exhibiting diverse physiological and pharmacological properties has received strong experimental support. Transmembrane topologies and patterns of the pore-facing residues are conserved in P-loop channels that include high-selective cation channels and certain ligand-gated channels. X-ray structures of bacterial K+ channels, KcsA, MthK and KvAP, help to understand structure-function relationships of other P-loop channels. Data on binding sites and mechanisms of action of ligands of K+, Na+, Ca2+ and glutamate gated ion channels are considered in view of their possible structural similarity to the bacterial K+ channels. Emphasized are structural determinants of ligand-receptor interactions within the channels and mechanisms of state-dependent action of the ligands.
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