Abstract
Rational drug discovery strategy requires a design of small molecules as candidate drugs which can specifically inhibit a target protein or any other macromolecule and effectively interfere in a defined physiological process. One of the important bacterial protein targets aimed toward developing new antibiotics is peptidyl-tRNA hydrolase (Pth). The discovery that cytarabine, a known anticancer drug, binds to Pth from Acinetobacter baumannii in a cleft located away from the catalytic site of this enzyme, published in Biochemical Journal, opens up interesting new avenues for drug design. An approach involving crystallographic identification of multiple ligand-binding sites on a target protein surface could enable iterative optimization of multiple high-affinity ligands, which may synergistically interfere in the target function with enhanced effect.
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