Synthesis, 1H NMR structure, and activity of a three-disulfide-bridged maurotoxin analog designed to restore the consensus motif of scorpion toxins.

@article{Fajloun2000Synthesis1N,
  title={Synthesis, 1H NMR structure, and activity of a three-disulfide-bridged maurotoxin analog designed to restore the consensus motif of scorpion toxins.},
  author={Ziad Fajloun and Gilles Ferrat and Edmond Carlier and M. Fathallah and Chantal Lecomte and Guillaume Sandoz and Eric di Luccio and Kamel Mabrouk and Christian Legros and Herv{\'e} Darbon and Herv{\'e} Rochat and Jean Marc Sabatier and Michel De Waard},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 18},
  pages={13605-12}
}
Maurotoxin (MTX) is a 34-residue toxin that has been isolated from the venom of the chactidae scorpion Scorpio maurus palmatus. The toxin displays an exceptionally wide range of pharmacological activity since it binds onto small conductance Ca(2+)-activated K(+) channels and also blocks Kv channels (Shaker, Kv1.2 and Kv1.3). MTX possesses 53-68% sequence identity with HsTx1 and Pi1, two other K(+) channel short chain scorpion toxins cross-linked by four disulfide bridges. These three toxins… CONTINUE READING