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Fig. 4 | Parasites & Vectors

Fig. 4

From: Drug targeting of aminoacyl-tRNA synthetases in Anopheles species and Aedes aegypti that cause malaria and dengue

Fig. 4

The structural analysis of the binding site in the phenylanalyl-tRNA synthetase from An. culicifacies in comparison with P. vivax and H. sapiens. a The three-dimensional crystal structure of the superimposed phenylanalyl-tRNA synthetase from An. culicifacies (built structure model, this study), P. vivax (PDB ID: 7BYG), and H. sapiens (PDB ID: 3L4G) are shown with bound inhibitor BRD1389 (in red). In the same figure chemical structure of the inhibitor BRD1389 is also depicted. b The key residues within 4 Å range of the BRD1389 binding cavity are shown for Pv (yellow), Hs (blue), and Ac (purple). c Multiple sequence alignment of the BRD1389 interacting residues is shown, with the key residues marked in red box. The IC50 value for the Pf-, Pv- and Hs-FRS are shown in µM range [35]. Pv: P. vivax; Hs: H. sapiens; Ac: An. culicifacies; As; An. stephensi; Am: An. minimus; Ag: An. gambiae; Ae: Ae. aegypti

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