Structural Basis of HIV-1 Inhibition by Nucleotide-Competing Reverse Transcriptase Inhibitor INDOPY-1 | Zendy

Francesc X. Ruiz | Zendy; Anthony N. Hoang | Zendy; Kalyan Das | Zendy; Eddy Arnold | Zendy

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Structural Basis of HIV-1 Inhibition by Nucleotide-Competing Reverse Transcriptase Inhibitor INDOPY-1

Author(s) -

Francesc X. Ruiz,

Anthony N. Hoang,

Kalyan Das,

Eddy Arnold

Publication year - 2019

Publication title -

journal of medicinal chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.01

H-Index - 261

eISSN - 1520-4804

pISSN - 0022-2623

DOI - 10.1021/acs.jmedchem.9b01289

Subject(s) - reverse transcriptase , chemistry , nucleotide , enzyme , nucleoside reverse transcriptase inhibitor , dna , nucleoside , reverse transcriptase inhibitor , dna polymerase , human immunodeficiency virus (hiv) , polymerase , nucleotidyltransferase , binding site , stereochemistry , virology , biochemistry , polymerase chain reaction , rna , biology , gene

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.

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