Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom.

@article{Nicastro2003SolutionSO,
  title={Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom.},
  author={G. Nicastro and L. Franzoni and C. de Chiara and A. Mancin and J. R. Giglio and A. Spisni},
  journal={European journal of biochemistry},
  year={2003},
  volume={270 9},
  pages={
          1969-79
        }
}
  • G. Nicastro, L. Franzoni, +3 authors A. Spisni
  • Published 2003
  • Biology, Medicine
  • European journal of biochemistry
  • Crotamine is a component of the venom of the snake Crotalus durissus terrificus and it belongs to the myotoxin protein family. It is a 42 amino acid toxin cross-linked by three disulfide bridges and characterized by a mild toxicity (LD50 = 820 micro g per 25 g body weight, i.p. injection) when compared to other members of the same family. Nonetheless, it possesses a wide spectrum of biological functions. In fact, besides being able to specifically modify voltage-sensitive Na+ channel, it has… CONTINUE READING
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