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. 1998 Apr 3;280(5360):106-9.
doi: 10.1126/science.280.5360.106.

Structural conservation in prokaryotic and eukaryotic potassium channels

R MacKinnon  1 , S L Cohen, A Kuo, A Lee, B T Chait
Affiliations

Structural conservation in prokaryotic and eukaryotic potassium channels

R MacKinnon et al. Science. .

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.

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Comment in

  • The vision of the pore.
    Armstrong C. Armstrong C. Science. 1998 Apr 3;280(5360):56-7. doi: 10.1126/science.280.5360.56. Science. 1998. PMID: 9556453 No abstract available.
  • A vision of the pore.
    Bakker-Grunwald T. Bakker-Grunwald T. Science. 1998 Aug 21;281(5380):1146. doi: 10.1126/science.281.5380.1143h. Science. 1998. PMID: 9735029 No abstract available.

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