ArticleChemical biology & drug design2012
Structural basis of the allosteric inhibitor interaction on the HIV-1 reverse transcriptase RNase H domain.
Article in Chemical biology & drug design, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Design, Synthesis and Biological Evaluation of 3-Hydrazonoindolin-2-one Derivatives as Novel HIV-1 RNase H Inhibitors.Molecules (Basel, Switzerland) · 2025Article
- Synthesis and Applications of Nitrogen-Containing Heterocycles as Antiviral Agents.Molecules (Basel, Switzerland) · 2022Review
- Flavonoids and Acid-Hydrolysis derivatives ofJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Retroviral RNase H: Structure, mechanism, and inhibition.The Enzymes · 2021Review
- 2-(Arylamino)-6-(trifluoromethyl)nicotinic Acid Derivatives: New HIV-1 RT Dual Inhibitors Active on Viral Replication.Molecules (Basel, Switzerland) · 2020Article
- 1,2,4-Triazolo[1,5-Molecules (Basel, Switzerland) · 2020Article
- Binding thermodynamics of metal ions to HIV-1 ribonuclease H domain.Journal of thermal analysis and calorimetry · 2019Article
- Article
- Identification of drivers for the metamorphic transition of HIV-1 reverse transcriptase.The Biochemical journal · 2017Article
- Preclinical Characterization of PC786, an Inhaled Small-Molecule Respiratory Syncytial Virus L Protein Polymerase Inhibitor.Antimicrobial agents and chemotherapy · 2017Article
- Entire-Dataset Analysis of NMR Fast-Exchange Titration Spectra: A MgThe journal of physical chemistry. B · 2016Article
- Free Energy-Based Virtual Screening and Optimization of RNase H Inhibitors of HIV-1 Reverse Transcriptase.ACS omega · 2016Article
- Structural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic Instability.Viruses · 2016Review
- Discovery of a small-molecule binder of the oncoprotein gankyrin that modulates gankyrin activity in the cell.Scientific reports · 2016Article
- Unfolding the HIV-1 reverse transcriptase RNase H domain--how to lose a molecular tug-of-war.Nucleic acids research · 2016Article
- Article
- Article
- Enzymatic Activities of RNase H Domains of HIV-1 Reverse Transcriptase with Substrate Binding Domains of Bacterial RNases H1 and H2.Molecular biotechnology · 2015Article
- The p66 immature precursor of HIV-1 reverse transcriptase.Proteins · 2014Article
- Drug resistance in non-B subtype HIV-1: impact of HIV-1 reverse transcriptase inhibitors.Viruses · 2014Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
HIV-1 reverse transcriptase (RT) has been an attractive target for the development of antiretroviral agents. Although this enzyme is bi-functional, having both DNA polymerase and ribonuclease H (RNH) activities, there is no clinically approved inhibitor of the RNH activity. Here, we characterize the structural basis and molecular interaction of an allosteric site inhibitor, BHMP07, with the wild-type (WT) RNH fragment. Solution NMR experiments for inhibitor titration on WT RNH showed relatively wide chemical shift perturbations, suggesting a long-range conformational effect on the inhibitor interaction. Comparisons of the inhibitor-induced NMR chemical shift changes of RNH with those of RNH dimer, in the presence and absence of Mg(2+) , were performed to determine and verify the interaction site. The NMR results, with assistance of molecular docking, indicate that BHMP07 preferentially binds to a site that is located between the RNH active site and the region encompassing helices B and D (the 'substrate-handle region'). The interaction site is consistent with the previous proposed site, identified using a chimeric RNH (p15-EC) [Gong et al. (2011) Chem Biol Drug Des 77, 39-47], but with slight differences that reflect the characteristics of the amino acid sequences in p15-EC compared to the WT RNH.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.