Interacting sites of scorpion toxin ErgTx1 with hERG1 K+ channels.

@article{JimnezVargas2012InteractingSO,
  title={Interacting sites of scorpion toxin ErgTx1 with hERG1 K+ channels.},
  author={Juana Mar{\'i}a Jim{\'e}nez-Vargas and Rita Restano-Cassulini and Lourival Domingos Possani},
  journal={Toxicon : official journal of the International Society on Toxinology},
  year={2012},
  volume={59 6},
  pages={633-41}
}
Peptides purified from scorpion venoms were shown to interact with specific amino acid residues present in the outer vestibule of various sub-types of potassium channels, occluding the pore and causing a decrement of K(+) permeability through the membrane of excitable and non excitable cells. This communication describes the identification of several interacting sites of toxin ErgTx1, a toxin purified from the venom of the scorpion Centruroides noxius, with the human ERG1 K(+) channels, by… CONTINUE READING
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