A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity.

@article{Cotton1997APT,
  title={A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity.},
  author={J{\"o}el Cotton and Marcel Crest and Françoise Bouet and Nicola Alessandri and Maurice Gola and Eric Forest and Evert Karlsson and Olga Casta{\~n}eda and A. L. Harvey and Claudio Vita and Andr{\'e} M{\'e}nez},
  journal={European journal of biochemistry},
  year={1997},
  volume={244 1},
  pages={192-202}
}
The potassium channel toxin secreted by the sea anemone Bunodosoma granulifera (BgK) is a 37-amino-acid peptide containing three disulfide bridges. Because a synthetic peptide corresponding to the reported sequence of BgK was found not to fold properly, the sequence was determined again. The new sequence differed from the previous one in the C-terminal tetrapeptide, which contains two cysteines involved in disulfide bridging. The revised sequence is: V C R D W F K E T A C R H A K S L G N C R T… CONTINUE READING