HIV-1 reverse transcriptase ribonuclease H domain (HIV-1 RT RNase H)

HIV-1 reverse transcriptase ribonuclease H domain is a specialized enzyme domain located at the C-terminus of the p66 subunit in the HIV-1 reverse transcriptase heterodimer. The enzyme has two critical, spatially separated activities: DNA polymerase (which copies viral RNA into DNA) and RNase H (which degrades the RNA strand of RNA/DNA hybrids during reverse transcription)[1][3][4]. The RNase H domain is essential for proper processing and removal of RNA primers, ensuring successful synthesis and integration of the viral DNA into the host genome[1][4]. RNase H function is required for HIV infectivity, making it an established and validated antiviral drug target. While the majority of HIV therapies target the RT polymerase, RNase H remains of interest for novel inhibitor development and overcoming drug resistance[1][2][4].

Other names

HIV-1 RNase HHIV-1 reverse transcriptase RNase H domainRNase H of HIV-1 reverse transcriptase

Inhibition of RNA cleavage in RNA/DNA hybrids, thus blocking conversion of viral RNA into DNA and interfering with viral replication. Blockade of reverse transcription, which prevents HIV-1 from integrating into host DNA[1][2].