Animal toxins acting on ion channels of excitable cells are principally highly potent short peptides that are present in limited amounts in the venoms of various unrelated species, such as scorpions, snakes, sea anemones, spiders, insects, marine cone snails and worms. These toxins have been used extensively as invaluable biochemical and pharmacological tools to characterize and discriminate between the various ion channel types that differ in ionic selectivity, structure and/or cell function. Alongside the huge molecular and functional diversity of ion channels, a no less impressive structural diversity of animal toxins has been indicated by the discovery of an increasing number of polypeptide folds that are able to target these ion channels. Indeed, it appears that these peptide toxins have evolved over time on the basis of clearly distinct architectural motifs, in order to adapt to different ion channel modulating strategies (pore blockers compared with gating modifiers). Herein, we provide an up-to-date overview of the various types of fold from animal toxins that act on ion channels selective for K+, Na+, Ca2+ or Cl− ions, with special emphasis on disulphide bridge frameworks and structural motifs associated with these peptide folds.
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Review Article| March 15 2004
Diversity of folds in animal toxins acting on ion channels
Michel DE WAARD;
Jean-Marc SABATIER 1
*Laboratoire Cellpep S.A., 13–15 Rue Ledru-Rollin, 13015 Marseille, France
‡Laboratoire de Biochimie, CNRS UMR 6560, Bd Pierre Dramard, 13916 Marseille, France
1To whom correspondence should be addressed (e-mail email@example.com).
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Stéphanie MOUHAT, Besma JOUIROU, Amor MOSBAH, Michel DE WAARD, Jean-Marc SABATIER; Diversity of folds in animal toxins acting on ion channels. Biochem J 15 March 2004; 378 (3): 717–726. doi: https://doi.org/10.1042/bj20031860
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