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Literature summary for 2.7.7.49 extracted from

  • Kirby, K.A.; Singh, K.; Michailidis, E.; Marchand, B.; Kodama, E.N.; Ashida, N.; Mitsuya, H.; Parniak, M.A.; Sarafianos, S.G.
    The sugar ring conformation of 4-ethynyl-2-fluoro-2-deoxyadenosine and its recognition by the polymerase active site of HIV reverse transcriptase (2011), Cell. Mol. Biol. (Noisy-le-grand), 57, 40-46.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
4'-ethynyl-2-fluoro-2'-deoxyadenosine a translocation defective RT inhibitor, able to inhibit both WT and multi-drug resistant strains of HIV several orders of magnitude, modeling of the ternary complex of HIV-1 RT/DNA/inhibitor, overview. The 4'-ethynyl group is stabilized in a hydrophobic pocket formed by enzyme residues Ala114, Tyr115, Phe160, Met184, and the aliphatic segment of Asp185 Human immunodeficiency virus 1
additional information nucleoside reverse transcriptase inhibitors mimic the natural dNTP substrate of the enzyme and bind to the 3'-primer terminus in the polymerase active site acting as chain terminators. A lack of a 3'-OH group promotes effective chain termination, but it also imparts a negative effect on the potency of the NRTI, including a diminished binding affinity for the RT target and decreased ability to be activated by cellular kinases. nucleoside reverse transcriptase inhibitors with 4'-substitutions and a 3'-OH are very effective at inhibiting both wild-type and multi-drug resistant strains of HIV, structure-function analysis, overview Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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-
-

Synonyms

Synonyms Comment Organism
HIV reverse transcriptase
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Human immunodeficiency virus 1