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• W2043456542 abstract "We report a methodology that combines affinity acetylation with MS analysis for accurate mapping of an inhibitor-binding site to a target protein. For this purpose, we used a known HIV-1 integrase inhibitor containing aryl di-O-acetyl groups (Acetylated-Inhibitor). In addition, we designed a control compound (Acetylated-Control) that also contained an aryl di-O-acetyl group but did not inhibit HIV-1 integrase. Examination of the reactivity of these compounds with a model peptide library, which collectively contained all 20 natural amino acids, revealed that aryl di-O-acetyl compounds effectively acetylate Cys, Lys, and Tyr residues. Acetylated-Inhibitor and Acetylated-Control exhibited comparable chemical reactivity with respect to these small peptides. However, these two compounds differed markedly in their interactions with HIV-1 integrase. In particular, Acetylated-Inhibitor specifically acetylated K173 at its inhibitory concentration (3 microM) whereas this site remained unrecognized by Acetylated-Control. Our data enabled creation of a detailed model for the integrase:Acetylated-Inhibitor complex, which indicated that the inhibitor selectively binds at an architecturally critical region of the protein. The methodology reported herein has a generic application for systems involving a variety of ligand-protein interactions." @default.
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• W2043456542 date "2004-04-26" @default.
• W2043456542 modified "2023-09-27" @default.
• W2043456542 title "Identification of an inhibitor-binding site to HIV-1 integrase with affinity acetylation and mass spectrometry" @default.
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• W2043456542 doi "https://doi.org/10.1073/pnas.0400873101" @default.
• W2043456542 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/406438" @default.
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