{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Machado LA"],"funding":["Coordenação de Aperfeiçoamento de Pessoal de Nível Superior"],"pagination":["170"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7468422"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7"],"pubmed_abstract":["HIV-1 integrase is the enzyme responsible for integrating the viral DNA into the host genome and is one of the main targets for antiretroviral therapy; however, there are documented cases of resistance against all the currently used integrase strand transfer inhibitors (INSTIs). While some resistance-related mutations occur near the inhibitor's binding site, the mutation N155H occurs on the opposite side of the drug-interacting Mg<sup>2+</sup> ions, thus, not interacting directly with the drug molecules and currently lacking an explanation for its resistance mechanism. Moreover, mutation N155H and the resistance-related mutation Q148H are mutually exclusive for unknown reasons. In the present study, we use molecular dynamics simulations to understand the impact of the N155H mutation in the"],"journal":["Frontiers in molecular biosciences"],"pubmed_title":["Evidence for Disruption of Mg<sup>2+</sup> Pair as a Resistance Mechanism Against HIV-1 Integrase Strand Transfer Inhibitors."],"pmcid":["PMC7468422"],"funding_grant_id":["(CAPES) - Finance Code 001"],"pubmed_authors":["Machado LA","Guimaraes ACR"],"additional_accession":[]},"is_claimable":false,"name":"Evidence for Disruption of Mg<sup>2+</sup> Pair as a Resistance Mechanism Against HIV-1 Integrase Strand Transfer Inhibitors.","description":"HIV-1 integrase is the enzyme responsible for integrating the viral DNA into the host genome and is one of the main targets for antiretroviral therapy; however, there are documented cases of resistance against all the currently used integrase strand transfer inhibitors (INSTIs). While some resistance-related mutations occur near the inhibitor's binding site, the mutation N155H occurs on the opposite side of the drug-interacting Mg<sup>2+</sup> ions, thus, not interacting directly with the drug molecules and currently lacking an explanation for its resistance mechanism. Moreover, mutation N155H and the resistance-related mutation Q148H are mutually exclusive for unknown reasons. In the present study, we use molecular dynamics simulations to understand the impact of the N155H mutation in the","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020","modification":"2026-04-14T03:10:10.566Z","creation":"2025-05-31T23:51:51.128Z"},"accession":"S-EPMC7468422","cross_references":{"pubmed":["32974383"],"doi":["10.3389/fmolb.2020.00170"]}}