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Fig. 3 | Parasites & Vectors

Fig. 3

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

Fig. 3

Halofuginone binding site in prolyl-tRNA synthetase from An. culicifacies in comparison with P. falciparum and H. sapiens. a Catalytic (C domain), anticodon binding and the C-terminal zinc-binding-like (Z domain) domains are marked on the three-dimensional crystal structure of holo-prolyl-tRNA synthetase from HsPRS (PDB: 4K88) (blue), PfPRS (PDB: 4YDQ3) (yellow), and AcPRS (built structure model, this study) (purple) are shown. Halofuginone (HF) is shown in red and phosphoamniophosphonic acid-adenylate ester (ANP) in green. The chemical structure of HF (halofuginone) is also shown (marked in red) in the same figure. b Structural superposition of the three-dimensional crystal structure with the key HF interacting residues is shown for P. falciparum, H. sapiens, and An. culicifacies. c Multiple sequence alignment of the HF binding site residues (red box) and the important secondary shell residues as determined from the known three-dimensional crystal structures across species is shown. Pf: P. falciparum; Cp: Cryptosporidium parvum; Tg: Toxoplasma gondii; Hs: H. sapiens; Ac: An. culicifacies; As; An. stephensi; Am: An. minimus; Ag: An. gambiae; Ae: Ae. aegypti

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