Pharmacology of Voltage-Gated Potassium Channels

Peptide toxins have been important tools for the analysis of the structure and function of potassium channels. They may bind with high specificity to voltage-gated potassium (Kv) channels and thereby alter their activity. This binding may either block the Kv channel pore or may modify Kv channel gating. This article discusses recent advances in our knowledge of Kv channel structure in relation to known toxin binding sites at the extracellular surface of Kv channels. Two principally different toxin receptor sites have been discovered: (i) the outer mouth of the pore; (ii) the S3/S4-linker region at some distance away from the pore.

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