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

Publication ,  Journal Article
Lee, S-Y; MacKinnon, R
Published in: Nature
July 8, 2004

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 surface. 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 interface.

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Published In

Nature

DOI

EISSN

1476-4687

Publication Date

July 8, 2004

Volume

430

Issue

6996

Start / End Page

232 / 235

Location

England

Related Subject Headings

  • Tryptophan
  • Spider Venoms
  • Potassium Channels, Voltage-Gated
  • Peptides
  • Molecular Sequence Data
  • Models, Biological
  • Membrane Lipids
  • Ion Channel Gating
  • General Science & Technology
  • Fluorescence
 

Citation

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Lee, S.-Y., & MacKinnon, R. (2004). A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom. Nature, 430(6996), 232–235. https://doi.org/10.1038/nature02632
Lee, Seok-Yong, and Roderick MacKinnon. “A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom.Nature 430, no. 6996 (July 8, 2004): 232–35. https://doi.org/10.1038/nature02632.
Lee, Seok-Yong, and Roderick MacKinnon. “A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom.Nature, vol. 430, no. 6996, July 2004, pp. 232–35. Pubmed, doi:10.1038/nature02632.
Journal cover image

Published In

Nature

DOI

EISSN

1476-4687

Publication Date

July 8, 2004

Volume

430

Issue

6996

Start / End Page

232 / 235

Location

England

Related Subject Headings

  • Tryptophan
  • Spider Venoms
  • Potassium Channels, Voltage-Gated
  • Peptides
  • Molecular Sequence Data
  • Models, Biological
  • Membrane Lipids
  • Ion Channel Gating
  • General Science & Technology
  • Fluorescence