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Literature summary for 3.4.23.47 extracted from

  • Triki, D.; Cano Contreras, M.E.; Flatters, D.; Visseaux, B.; Descamps, D.; Camproux, A.C.; Regad, L.
    Analysis of the HIV-2 proteases adaptation to various ligands characterization of backbone asymmetry using a structural alphabet (2018), Sci. Rep., 8, 710 .
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
additional information the ligand binding site is located at the interface between the two monomers and includes the catalytic triplet, Asp-Thr-Gly, conserved in all aspartic proteases. Detection of structural local asymmetry in the PR2 dimer complexed with a diversified set of ligands, quantification of the structural asymmetry of the PR2 set, overview Human immunodeficiency virus 2

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 2 P04584 Gag-Pol polyprotein; HIV-2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PR2 recognizes various non-homologous substrates (Gag and Pol polyproteins) at several cleavage sites and protease inhibitors Human immunodeficiency virus 2 ?
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 ?

Subunits

Subunits Comment Organism
homodimer
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 Human immunodeficiency virus 2

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
additional information PR2 is an aspartic protease corresponding to a C2-symmetric homodimer of 99 residues in each monomer. The ligand binding site is located at the interface between the two monomers and includes the catalytic triplet, Asp-Thr-Gly, conserved in all aspartic proteases. Detection of structural local asymmetry in the PR2 dimer complexed with a diversified set of ligands, global structural asymmetry of PR2 dimers, overview Human immunodeficiency virus 2
physiological function HIV PR2 is essential for hydrolysing the viral Gag and the Gag-Pol precursor polyproteins during the maturation of infectious viral particles Human immunodeficiency virus 2