STRUCTURAL CONSERVATION IN PROKARYOTIC AND EUKARYOTIC POTASSIUM CHANNELS

Toxins from scorpion venom interact with potassium channels. Resin-att ached, mutant K+ channels from Streptomyces lividans were used to scre en venom from Leiurus quinquestriatus hebraeus, and the toxins that in teracted with the channel were rapidly identified by mass spectrometry . One of the toxins, agitoxin2, was further studied by mutagenesis and radioligand binding. The results show that a prokaryotic K+ channel h as the same pore structure as eukaryotic K+ channels. This structural conservation, through application of techniques presented here, offers a new approach for K+ channel pharmacology.