Structural basis for the voltage-gated Na+ channel selectivity of the scorpion alpha-like toxin BmK M1.

@article{Ye2005StructuralBF,
  title={Structural basis for the voltage-gated Na+ channel selectivity of the scorpion alpha-like toxin BmK M1.},
  author={Xiang Ye and Frank Bosmans and Chong Li and Ying Zhang and Da-cheng Wang and Jan Tytgat},
  journal={Journal of molecular biology},
  year={2005},
  volume={353 4},
  pages={788-803}
}
Scorpion alpha-like toxins are proteins that act on mammalian and insect voltage-gated Na+ channels. Therefore, these toxins constitute an excellent target for examining the foundations that underlie their target specificity. With this motive we dissected the role of six critical amino acids located in the five-residue reverse turn (RT) and C-tail (CT) of the scorpion alpha-like toxin BmK M1. These residues were individually substituted resulting in 11 mutants and were subjected to a bioassay… CONTINUE READING