@article{f915f0583857401bbf4a90b3937e8c17,
title = "Structural Basis of HIV-1 Inhibition by Nucleotide-Competing Reverse Transcriptase Inhibitor INDOPY-1",
abstract = "HIV-1 reverse transcriptase (RT) is an essential enzyme, targeting half of approved anti-AIDS drugs. While nucleoside RT inhibitors (NRTIs) are DNA chain terminators, the nucleotide-competing RT inhibitor (NcRTI) INDOPY-1 blocks dNTP binding to RT. Lack of structural information hindered INDOPY-1 improvement. Here we report the HIV-1 RT/DNA/INDOPY-1 crystal structure, revealing a unique mode of inhibitor binding at the polymerase active site without involving catalytic metal ions. The structure may enable new strategies for developing NcRTIs.",
author = "Ruiz, {F. Xavier} and Anthony Hoang and Kalyan Das and Eddy Arnold",
note = "Funding Information: We are grateful to APS staff members for support and access to beamline 23-ID-D for data collection, to Dr. Sergio Martinez and Dr. Dirk Jochmans for helpful discussions, and to Natalie Losada for assistance with figures. INDOPY-1 was obtained through the NIH AIDS Reagent Program, Division of AIDS, NIAID, NIH (from Tibotec BVBA). This work was supported by the National Institutes of Health MERIT Award R37 AI027690 to E.A. Funding Information: We are grateful to APS staff members for support and access to beamline 23-ID-D for data collection, to Dr. Sergio Martinez and Dr. Dirk Jochmans for helpful discussions, and to Natalie Losada for assistance with figures. INDOPY-1 was obtained through the NIH AIDS Reagent Program, Division of AIDS, NIAID, NIH (from Tibotec BVBA). This work was supported by the National Institutes of Health MERIT Award R37 AI027690 to E.A. Publisher Copyright: Copyright {\textcopyright} 2019 American Chemical Society.",
year = "2019",
month = nov,
day = "14",
doi = "10.1021/acs.jmedchem.9b01289",
language = "English (US)",
volume = "62",
pages = "9996--10002",
journal = "Journal of medicinal chemistry",
issn = "0022-2623",
publisher = "American Chemical Society",
number = "21",
}