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• W1973602142 abstract "Using the crystal structure of the first complex of the HIV-1 integrase catalytic core domain with an inhibitor bound to the active site, structural models for the interaction of various inhibitors with integrase were generated by computational docking. For the compound of the crystallographic study, binding modes unaffected by crystal packing have recently been proposed. Although a large search region was used for the docking simulations, the ligands investigated here are found to bind preferably in similar ways close to the active site. The binding site is formed by residues 64-67, 116, 148, 151-152, 155-156, and 159, as well as by residue 92 in case of the largest ligand of the series. The coherent picture of possible interactions of small-molecule inhibitors at the active site provides an improved basis for structure-based ligand design. The recurring motif of tight interaction with the two lysine residues 156 and 159 is suggested to be of prime importance." @default.
• W1973602142 created "2016-06-24" @default.
• W1973602142 creator A5035429952 @default.
• W1973602142 creator A5042202366 @default.
• W1973602142 creator A5046011728 @default.
• W1973602142 date "2000-10-12" @default.
• W1973602142 modified "2023-09-27" @default.
• W1973602142 title "Active Site Binding Modes of HIV-1 Integrase Inhibitors" @default.
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• W1973602142 doi "https://doi.org/10.1021/jm000194t" @default.
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