Structural Conservation in Prokaryotic and Eukaryotic Potassium Channels

See allHide authors and affiliations

Science  03 Apr 1998:
Vol. 280, Issue 5360, pp. 106-109
DOI: 10.1126/science.280.5360.106

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


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.

  • * To whom correspondence should be addressed. E-mail: mackinn{at}

View Full Text

Stay Connected to Science