Touching the heart of HIV-1 drug resistance: the fingers close down on the dNTP at the polymerase active site.
Comparison of the recently solved structure of HIV-1 reverse transcriptase (RT)-DNA-dNTP ternary complex with the previously solved structure of RT-DNA binary complex suggests mechanisms by which the HIV-1 RT becomes resistant to nucleoside-analog inhibitors, drugs currently used in the treatment of AIDS.
D019380:Anti-HIV Agents / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D004279:DNA, Viral / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D003838:Deoxyadenine Nucleotides / Q000737:chemistry* / Q000378:metabolism; D003848:Deoxyguanine Nucleotides / Q000737:chemistry* / Q000378:metabolism; D005544:Forecasting; D054303:HIV Reverse Transcriptase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D046911:Macromolecular Substances; D008958:Models, Molecular