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Fig. 5 | Journal of Venomous Animals and Toxins including Tropical Diseases

Fig. 5

From: Sequence analysis of the cDNA encoding for SpCTx: a lethal factor from scorpionfish venom (Scorpaena plumieri)

Fig. 5

Three-dimensional modeled structure of Sp-CTx. The Sp-CTX modeled structures are shown in cartoon format. a Modeled structure showing interactions between Sp-CTx subunits; Sp-CTx-α (gray) and Sp-CTx-β (blue). Identification of the N-terminal domains; MACPF/CDC, FAT, THX and PRYSPRY, the transmembrane α-helices TMH1 and TMH2, the amphiphilic α-helices (red) of Sp-CTx-α and β-chains. b The structure of Sp-CTx aligned with SNTX (Protein Data Bank ID code 4WVM) and schematic representation of α-subunits (gray) on the left and β-subunits (blue) on the right. Lighter tones depict the structure of SNTX. c Highlighted interface region within the heterodimer in the MACPF/CDC with β-strands numbered according to their position in the central β-sheet. The β4-α6 loop is shown in pink, the conserved G208 (Sp-CTx-α) is shown as a red sphere. Hydrogen bonds between the residues F206 and K207 of strand-β4 (Sp-CTx-α) and T53, F54, E55 of strand-β1 (Sp-CTx-β) are displayed as yellow dashed lines. d The interface region of prepore in MACPF/CDC. The β4-α6 loop is colored orange, the conserved G209 (Sp-CTx-β) is shown as a red sphere. Hydrogen bonds between residues T218 in β4- α6 loop (Sp-CTx-β) and D52, T53 of strand-β1 (Sp-CTx-α) are shown as yellow dashed lines. Figures were generated using Pymol (v1.7.0.0), (http://www.pymol.org/; Delano Scientific LLC, South San Francisco, CA)

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