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. 2011 Aug 24;6(8):e23520. doi: 10.1371/journal.pone.0023520

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Rowe et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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CvIV4 is aligned with ODI, BmK MI, AahII and LqhIII, Old World α-toxins that slow the fast inactivation of Na_v1.7. The biological activity of CvIV4 is similar to these peptides, but its primary structure is not. Gaps were introduced to align cysteine residues (white font with black background). Hydrophobic residues (dark shaded background) that are critical for α-toxin structure and function are conserved in CvIV4 at positions 5, 14, 22, 36, 43 and 49 [28]. CvIV4 shares a lysine (light shaded background) with AahII (position 60) that is critical for the biological activity of AahII [29]. Additional amino acids that are identical among toxins are marked with an asterisk (*). GenBank accession numbers: CvIV4 (JF938594), ODI (P84646), BmK MI (P45697), AahII (P01484), LqhII (P59355). MAFFT version 6 used for sequence alignment (http://mafft.cbrc.jp/alignment/software/).