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Structural Conservation in Prokaryotic and Eukaryotic Potassium Channels

R MacKinnon, S L Cohen, A Kuo, A Lee, B T Chait

Science. 1998 Apr 3;280(5360):106-9.

PMID: 9525854

Abstract:

Toxins from scorpion venom interact with potassium channels. Resin-attached, mutant K+ channels from Streptomyces lividans were used to screen venom from Leiurus quinquestriatus hebraeus, and the toxins that interacted 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 has 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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR4242664 Charybdotoxin, recombinant from Leiurus quinquestriatus hebraeus Charybdotoxin, recombinant from Leiurus quinquestriatus hebraeus Price
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