ArticleNucleic acids research2009
Specificity of LTR DNA recognition by a peptide mimicking the HIV-1 integrase {alpha}4 helix.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Classification and Design of HIV-1 Integrase Inhibitors Based on Machine Learning.Computational and mathematical methods in medicine · 2021Article
- Article
- A targeted DNA substrate mechanism for the inhibition of HIV-1 integrase by inhibitors with antiretroviral activity.FEBS open bio · 2016Article
- A homology model of HIV-1 integrase and analysis of mutations designed to test the model.Journal of molecular biology · 2013Article
- Localization of ASV integrase-DNA contacts by site-directed crosslinking and their structural analysis.PloS one · 2011Article
- The HIV-1 integrase α4-helix involved in LTR-DNA recognition is also a highly antigenic peptide element.PloS one · 2010Article
- Structure-based modeling of the functional HIV-1 intasome and its inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Retroviral Integrase Structure and DNA Recombination Mechanism.Microbiology spectrumArticle
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Authors and funding
6 authors.
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Abstract
HIV-1 integrase integrates retroviral DNA through 3'-processing and strand transfer reactions in the presence of a divalent cation (Mg(2+) or Mn(2+)). The alpha4 helix exposed at the catalytic core surface is essential to the specific recognition of viral DNA. To define group determinants of recognition, we used a model composed of a peptide analogue of the alpha4 helix, oligonucleotides mimicking processed and unprocessed U5 LTR end and 5 mM Mg(2+). Circular dichroism, fluorescence and NMR experiments confirmed the implication of the alpha4 helix polar/charged face in specific and non-specific bindings to LTR ends. The specific binding requires unprocessed LTR ends-i.e. an unaltered 3'-processing site CA downward arrowGT3'-and is reinforced by Mg(2+) (K(d) decreases from 2 to 0.8 nM). The latter likely interacts with the ApG and GpT3' steps of the 3'-processing site. With deletion of GT3', only persists non-specific binding (K(d) of 100 microM). Proton chemical shift deviations showed that specific binding need conserved amino acids in the alpha4 helix and conserved nucleotide bases and backbone groups at LTR ends. We suggest a conserved recognition mechanism based on both direct and indirect readout and which is subject to evolutionary pressure.
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