A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom

Seok-Yong Lee and Roderick MacKinnon ()
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Seok-Yong Lee: The Howard Hughes Medical Institute and Rockefeller University
Roderick MacKinnon: The Howard Hughes Medical Institute and Rockefeller University

Nature, 2004, vol. 430, issue 6996, 232-235

Abstract: Abstract Venomous animals produce small protein toxins that inhibit ion channels with high affinity. In several well-studied cases the inhibitory proteins are water-soluble and bind at a channel's aqueous-exposed extracellular surface1,2,3,4. Here we show that a voltage-sensor toxin (VSTX1) from the Chilean Rose Tarantula (Grammostola spatulata) reaches its target by partitioning into the lipid membrane. Lipid membrane partitioning serves two purposes: to localize the toxin in the membrane where the voltage sensor resides and to exploit the free energy of partitioning to achieve apparent high-affinity inhibition. VSTX1, small hydrophobic poisons and anaesthetic molecules reveal a common theme of voltage sensor inhibition through lipid membrane access. The apparent requirement for such access is consistent with the recent proposal that the sensor in voltage-dependent K+ channels is located at the membrane–protein interface5,6.

Date: 2004
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DOI: 10.1038/nature02632

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