Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Biophys J. 2000 Aug;79(2):776-87.

Mechanisms of maurotoxin action on Shaker potassium channels.

Author information

  • 1Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242, USA.

Abstract

Maurotoxin (alpha-KTx6.2) is a toxin derived from the Tunisian chactoid scorpion Scorpio maurus palmatus, and it is a member of a new family of toxins that contain four disulfide bridges (, Eur. J. Biochem. 254:468-479). We investigated the mechanism of the maurotoxin action on voltage-gated K(+) channels expressed in Xenopus oocytes. Maurotoxin blocks the channels in a voltage-dependent manner, with its efficacy increasing with greater hyperpolarization. We show that an amino acid residue in the external mouth of the channel pore segment that is known to be involved in the actions of other peptide toxins is also involved in maurotoxin's interaction with the channel. We conclude that, despite the unusual disulfide bridge pattern, the mechanism of the maurotoxin action is similar to those of other K(+) channel toxins with only three disulfide bridges.

PMID:
10920011
[PubMed - indexed for MEDLINE]
PMCID:
PMC1300977
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for PubMed Central
    Loading ...
    Write to the Help Desk