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Biophys J, August 2000, p. 776-787, Vol. 79, No. 2

Mechanisms of Maurotoxin Action on Shaker Potassium Channels

Vladimir Avdonin,* Brian Nolan,* Jean-Marc Sabatier,dagger Michel De Waard,Dagger and Toshinori Hoshi*

 *Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242 USA; and  Dagger Laboratoire de Neurobiologie des Canaux Ioniques and  dagger Laboratoire de Biochimie, UMR 6560, Faculté de Médecine Nord, Institut Fédératif Jean Roche, Institut National de la Santé et de la Recherche Médicale U464, 13916 Marseille Cedex 20, France

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 (Selisko et al., 1998, 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.

Biophys J, August 2000, p. 776-787, Vol. 79, No. 2
© 2000 by the Biophysical Society   0006-3495/00/08/776/12  $2.00


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