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

  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},
  volume={59 6},
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
3 Citations
30 References
Similar Papers


Publications referenced by this paper.
Showing 1-10 of 30 references

Solution structure for CnErg1 (Ergtoxin), a HERG specific scorpion toxin

  • A. M. Torres, P. Bansal, P. F. Alewood, J. A. Bursill, P. W. Kuchel, J. I. Vandenburg
  • FEBS Lett
  • 2003
Highly Influential
5 Excerpts

Amino acid sequence determination and chemical synthesis of CllErg1 (ã-KTx1.5), a Kþ channel blocker peptide isolated from the scorpion Centruroides limpidus limpidus

  • F. I. Coronas, C. Balderas, L. Pardo- Lopez, L. D. Possani, G. B. Gurrola
  • J. Braz. Chem. Soc
  • 2005
1 Excerpt

Similar Papers

Loading similar papers…