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Literature summary for 3.4.23.47 extracted from

  • Triki, D.; Billot, T.; Visseaux, B.; Descamps, D.; Flatters, D.; Camproux, A.C.; Regad, L.
    Exploration of the effect of sequence variations located inside the binding pocket of HIV-1 and HIV-2 proteases (2018), Sci. Rep., 8, 5789 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
medicine the HIV proteases are effective therapeutic targets for treating HIV infection because of the essential role in hydrolysing the viral Gag and Gag-Pol precursor polyprotein during infectious viral particle maturation Human immunodeficiency virus 2

Cloned(Commentary)

Cloned (Comment) Organism
HIV protease PR2, sequence comparisons with PR1 Human immunodeficiency virus 2

Inhibitors

Inhibitors Comment Organism Structure
additional information HIV-2 protease (PR2) is naturally resistant to most FDA approved HIV-1 protease inhibitors (PIs), a major antiretroviral class. Comparison of the HIV-1 protease (PR1) and HIV-2 protease (PR2) binding pockets extracted from structures complexed with 12 ligands, overview. Structural comparison of PR1 and PR2 pockets highlight structural changes induced by their sequence variations. PR2 pockets are more hydrophobic with more oxygen atoms and fewer nitrogen atoms than PR1 pockets. Specifically, substitutions at residues 31, 46, and 82 induce structural changes in their main-chain atoms that can affect PI binding in PR2. Substitutions in the PR1 and PR2 pockets can modify PI binding and flap flexibility, which might underlie PR2 resistance against PIs Human immunodeficiency virus 2

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 2 P04584 Gag-Pol polyprotein; HIV-2
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Synonyms

Synonyms Comment Organism
HIV-2 protease
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 Human immunodeficiency virus 2
PR2
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 Human immunodeficiency virus 2

General Information

General Information Comment Organism
evolution HIV proteases PR1 and PR2 share only approximately 50% of sequence identity but they exhibit a similar global fold Human immunodeficiency virus 2
additional information comparison of the HIV-1 protease and HIV-2 protease binding pockets extracted from structures complexed with 12 ligands, overview Human immunodeficiency virus 2