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• W2120525208 abstract "Abstract Identifying potential ligand binding sites on a protein surface is an important first step for targeted structure‐based drug discovery. While performing control experiments with Escherichia coli peptide deformylase (PDF), we noted that the organic solvents used to solubilize some ligands perturbed many of the same resonances in PDF as the small molecule inhibitors. To further explore this observation, we recorded 15 N HSQC spectra of E. coli peptide deformylase (PDF) in the presence of trace quantities of several simple organic solvents (acetone, DMSO, ethanol, isopropanol) and identified their sites of interaction from local perturbation of amide chemical shifts. Analysis of the protein surface structure revealed that the ligand‐induced shift perturbations map to the active site and one additional surface pocket. The correlation between sites of solvent and inhibitor binding highlights the utility of organic solvents to rapidly and effectively validate and characterize binding sites on proteins prior to designing a drug discovery screen. Further, the solvent‐induced perturbations have implications for the use of organic solvents to dissolve candidate ligands in NMR‐based screens." @default.
• W2120525208 created "2016-06-24" @default.
• W2120525208 creator A5043274932 @default.
• W2120525208 creator A5060042170 @default.
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• W2120525208 date "2002-07-01" @default.
• W2120525208 modified "2023-10-11" @default.
• W2120525208 title "Mapping the surface of Escherichia coli peptide deformylase by NMR with organic solvents" @default.
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• W2120525208 doi "https://doi.org/10.1110/ps.0203402" @default.
• W2120525208 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2373664" @default.
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• W2120525208 hasPublicationYear "2002" @default.
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