作者: C. K. Shih , J. M. Rose , G. L. Hansen , J. C. Wu , A. Bacolla
关键词: Enzyme inhibitor 、 Virus 、 Virology 、 Biology 、 Enzyme 、 Amino acid 、 Binding site 、 Tyrosine 、 Reverse transcriptase 、 Affinity label
摘要: Abstract Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), an important therapeutic target in the treatment of AIDS, is effectively inhibited by a class nonnucleoside analog compounds that includes nevirapine (BI-RG-587) and tetrahydroimidazo[4,5,1-jk]-[1,4]benzodiazepin-2(1H)-one -thione. We show both tyrosine residues at positions 181 188 flanking putative catalytic site HIV-1 RT are required for sensitivity enzyme to these compounds. HIV-2 RT, which does not have tyrosines positions, resistant inhibitors. Substitution amino acid position or into results while retaining 3'-azido-2',3'-dideoxythymidine triphosphate. substituted with acids 176-190 from acquires