Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is an essential enzyme for HIV replication which converts the single-stranded viral RNA into a double-stranded DNA, suitable for integration into the host cell genome (Telesnitsky and Goff 1997). Heterodimeric p66/p51 HIV-1 RT (Fig. 19.1) has both synthetic (DNA polymerase) and degradative activities (ribonuclease H or RNase H), located at the N- and C-terminus of its p66 subunit, respectively. During HIV-1 replication, a complicated series of protein–protein and protein–nucleic acid interactions occur, each with the potential to be targeted by a small-molecule antagonist which might be developed into a potent therapeutic agent. Given the problem of increasing resistance against anti-HIV drugs currently in clinical use and the continued need to identify new drug targets, enzymatic activities and interactions, protein folding, and disruption of nucleic-acid structure are areas where detailed studies promise to unveil novel approaches with the potential for therapeutic intervention.
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Wendeler, M., Miller, J.T., Le Grice, S.F. (2009). Human Immunodeficiency Virus Reverse Transcriptase. In: Raney, K., Gotte, M., Cameron, C. (eds) Viral Genome Replication. Springer, Boston, MA. https://doi.org/10.1007/b135974_19
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