Residues subjected to positive selection and species or group-specific replacements on 3D models of Anopheles gambiae female serine proteases. Only residues that are within 15 Å and/or have a position that is compatible with a role in the substrate recognition and/or binding, are represented. The catalytic triad is coloured by element. a) AGAP005194: 5 out of the 8 residues subjected to positive selection (Table 2) are reported (green). The single A. merus specific residue is > 20 Å distant from the catalytic serine, exposed to the solvent and lies on the face diametrically opposed to that of the catalytic triad (not shown); b) AGAP005195: positive selected residues are in green; group-specific (A. merus + A. melas) residues are in orange; residues that are both group-specific and subjected to positive selection are in red. Codon 71 is shown in brown; c) AGAP005196: positive selected residues are in green; group-specific (A. melas-like) residues are in orange; d) Superimposition of the 3 proteases models: AGAP005194 in brown, AGAP005195 in orange, AGAP005196 in yellow, residues at position 156 in red (the catalytic serines of the three proteases are reported for reference only). A zoom of the protease specificity pocket (circled), which is occupied by the aromatic ring of the AGAP005194 phenylalanine (phe) in position 156 (in cyan). The less bulky valines (VAL) of AGAP005195 and AGAP005196 are reported in light and dark blue, respectively.
Mancini et al. BMC Evolutionary Biology 2011 11:72 doi:10.1186/1471-2148-11-72