Search for new therapeutics against HIV-1 via dual inhibition of RNase H and integrase: Current status and future challenges
Reverse transcriptase and integrase are key enzymes that play a pivotal role in HIV-1 viral maturation and replication. Reverse transcriptase consists of two active sites: RNA-dependent DNA polymerase and RNase H. The catalytic domains of integrase and RNase H share striking similarity, comprising t...
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| Main Authors: | , , , , , , , |
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| Format: | Article |
| Published: |
Future Medicine Ltd.
2021
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| Subjects: | |
| Online Access: | http://eprints.utm.my/id/eprint/94876/ http://dx.doi.org/10.4155/fmc-2020-0257 |
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| Summary: | Reverse transcriptase and integrase are key enzymes that play a pivotal role in HIV-1 viral maturation and replication. Reverse transcriptase consists of two active sites: RNA-dependent DNA polymerase and RNase H. The catalytic domains of integrase and RNase H share striking similarity, comprising two aspartates and one glutamate residue, also known as the catalytic DDE triad, and a Mg2+ pair. The simultaneous inhibition of reverse transcriptase and integrase can be a rational drug discovery approach for combating the emerging drug resistance problem. In the present review, the dual inhibition of RNase H and integrase is systematically discussed, including rationality of design, journey of development, advancement and future perspective. |
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