A potent toxin present in the venom of a fish-hunting cone snail is a minimized insulin (Con-Ins G1) lacking key residues involved in the receptor binding of most insulins. New data show that Con-Ins G1 nevertheless binds potently to the human insulin receptor, owing to a rearrangement that compensates for the lack of a critical binding residue.
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P.D.M. is an external consultant for Novo Nordisk A/S, Måløv, Denmark.
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De Meyts, P. Structural basis for the poisonous activity of a predator's venom insulin. Nat Struct Mol Biol 23, 872–874 (2016). https://doi.org/10.1038/nsmb.3304
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DOI: https://doi.org/10.1038/nsmb.3304
