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Literature summary extracted from

  • Triki, D.; Fartek, S.; Visseaux, B.; Descamps, D.; Camproux, A.C.; Regad, L.
    Characterizing the structural variability of HIV-2 protease upon the binding of diverse ligands using a structural alphabet approach (2018), J. Biomol. Struct. Dyn., 37, 4658-4670 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.23.47 drug development HIV-2 protease is an important drug target Human immunodeficiency virus 2

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.23.47 analysis of 19 ligand-bound wild-type enzyme crystal structures, overview. Mutation K57L is experimentally introduced in 8 structures to help the crystallographic process Human immunodeficiency virus 2

Protein Variants

EC Number Protein Variants Comment Organism
3.4.23.47 K57L site-directed mutagenesis, the mutation is experimentally introduced to help the crystallographic process Human immunodeficiency virus 2

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.47 additional information comparison of 19 ligand-bound enzyme structures to localize structural asymmetry specific to particular ligands and the one conserved across most PR2 structures, detailed overview. Localization of structural variability induced by PR2 intrinsic flexibility Human immunodeficiency virus 2

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.47 Human immunodeficiency virus 2 P04584 Gag-Pol polyprotein; HIV-2
-

Subunits

EC Number Subunits Comment Organism
3.4.23.47 homodimer
-
 Human immunodeficiency virus 2

Synonyms

EC Number Synonyms Comment Organism
3.4.23.47 HIV-2 protease
-
 Human immunodeficiency virus 2
3.4.23.47 PR2
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 Human immunodeficiency virus 2

General Information

EC Number General Information Comment Organism
3.4.23.47 additional information 77% of PR2 positions are structurally variable, meaning they exhibit different local conformations in PR2 structures, structural variability of the binding pocket and PR2-ligand interactions, ligand binding structure analysis, detailed overview. The catalytic position is D25A/B Human immunodeficiency virus 2