Application | Comment | Organism |
---|---|---|
drug development | HIV-2 protease is an important drug target | Human immunodeficiency virus 2 |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
K57L | site-directed mutagenesis, the mutation is experimentally introduced to help the crystallographic process | Human immunodeficiency virus 2 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 2 | P04584 | Gag-Pol polyprotein; HIV-2 | - |
Subunits | Comment | Organism |
---|---|---|
homodimer | - |
Human immunodeficiency virus 2 |
Synonyms | Comment | Organism |
---|---|---|
HIV-2 protease | - |
Human immunodeficiency virus 2 |
PR2 | - |
Human immunodeficiency virus 2 |
General Information | Comment | Organism |
---|---|---|
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 |