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Characterization of the binding site for nevirapine (BI-RG-587), a nonnucleoside inhibitor of human immunodeficiency virus type-1 reverse transcriptase

1991; Elsevier BV; Volume: 266; Issue: 22 Linguagem: Inglês

10.1016/s0021-9258(18)98737-5

1083-351X

K.A. Cohen, John Hopkins, Richard H. Ingraham, Christopher Pargellis, Joseph C. Wu, D Palladino, P Kinkade, Thomas C. Warren, Sheri Rogers, Julian Adams,

Click Chemistry and Applications

Nevirapine (BI-RG-587) is a potent and specific non-nucleoside inhibitor of human immunodeficiency virus type-1 reverse transcriptase. The compound is non-competitive with respect to template, primer, and nucleoside triphosphates indicating that BI-RG-587 does not act directly at the catalytic site. The binding site for this inhibitor was investigated by employing an azido photoaffinity analogue, BI-RJ-70, to covalently label the enzyme. The resulting photoadduct was subjected to enzymatic digestion by trypsin and endoproteinase lys-C and a single, highly labeled peptide was identified as residues 174-199. Sequencing of this peptide identified Tyr-181 and Tyr-188 as labeled residues.