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- W2030537953 abstract "Fighting bacterial resistance is a challenging task in the field of medicinal chemistry. DNA gyrase represents a validated antibacterial target and has drawn much interest in recent years. By a structure-based approach we have previously discovered compound 1, an indolinone derivative, possessing inhibitory activity against DNA gyrase. In the present paper, a detailed biophysical characterization of this inhibitor is described. Using mass spectrometry, NMR spectroscopy, and fluorescence experiments we have demonstrated that compound 1 binds reversibly to the ATP-binding site of the 24 kDa N-terminal fragment of DNA gyrase B from Escherichia coli (GyrB24) with low micromolar affinity. Based on these data, a plausible molecular model of compound 1 in the active site of GyrB24 was constructed. The predicted binding mode explains the competitive inhibitory mechanism with respect to ATP and forms a useful basis for further development of potent DNA gyrase inhibitors." @default.
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- W2030537953 date "2006-11-01" @default.
- W2030537953 modified "2023-10-16" @default.
- W2030537953 title "Biophysical characterization of an indolinone inhibitor in the ATP-binding site of DNA gyrase" @default.
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- W2030537953 doi "https://doi.org/10.1016/j.bbrc.2006.08.172" @default.
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