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Literature summary for 3.1.26.13 extracted from

  • Yang, F.; Zheng, G.; Fu, T.; Li, X.; Tu, G.; Li, Y.H.; Yao, X.; Xue, W.; Zhu, F.
    Prediction of the binding mode and resistance profile for a dual-target pyrrolyl diketo acid scaffold against HIV-1 integrase and reverse-transcriptase-associated ribonuclease H (2018), Phys. Chem. Chem. Phys., 20, 23873-23884 .
    View publication on PubMed

Application

Application Comment Organism
drug development the enzyme is a target for the development of effective dual HIV-1 IN and RNase H inhibitors Human immunodeficiency virus 1

Protein Variants

Protein Variants Comment Organism
D443A site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme Human immunodeficiency virus 1
D549A site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme Human immunodeficiency virus 1
E478A site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme Human immunodeficiency virus 1
K540A site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme Human immunodeficiency virus 1
W535A site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
additional information binding mode and resistance profile for a dual-target pyrrolyl diketo acid scaffold against HIV-1 integrase and reverse-transcriptase-associated ribonuclease H (RNase H), using wild-type and mutant enzymes, and detail energy components contribution of calculated binding free energies of studied inhibitors binding to HIV-1 IN and RNase H wild-types and mutants, overview Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
HIV-1
-

Synonyms

Synonyms Comment Organism
reverse-transcriptase-associated ribonuclease H
-
Human immunodeficiency virus 1
RNase H
-
Human immunodeficiency virus 1

General Information

General Information Comment Organism
malfunction two mutations in HIV-1 RNase H, Y501R and Y501W, result in a reduction of inhibitor potency, thus indicating their potential role in providing resistance to the inhibitor Human immunodeficiency virus 1