The disulfide bridges of toxin 2 from the venom of the scorpion Centruroides noxius Hoffmann were found by amino acid sequence determination of fragments of native toxin, produced by enzymatic cleavage and separated by high-performance liquid chromatography (HPLC). They are: Cys12-Cys65, Cys16-Cys41, Cys25-Cys46 and Cys29-Cys48. The coordinates of the X-ray diffraction structure of toxin variant 3 of C. sculpturatus [(1980) Proc. Natl. Acad. Sci. USA 77, 6496-6500] were used to construct a three-dimensional model of toxin 2. All the amino acid replacements were easily accommodated, and the modeled structure reveals a clustered pattern of sequence variation, which may help to identify residues responsible for functional differences among toxins of mammals and insects.
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Gurrola et al. (1994) studied this question.
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