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 1 |
Cloned (Comment) | Organism |
---|---|
HIV protease PR1, sequence comparisons with PR2 | Human immunodeficiency virus 1 |
Protein Variants | Comment | Organism |
---|---|---|
C67A | naturally occuring mutation | Human immunodeficiency virus 1 |
C95A | naturally occuring mutation | Human immunodeficiency virus 1 |
L33I | naturally occuring mutation | Human immunodeficiency virus 1 |
L63I | naturally occuring mutation | Human immunodeficiency virus 1 |
L76M | site-directed mutagenesis, mutant enzyme structure modelling | Human immunodeficiency virus 1 |
additional information | modelling of PR1 mutant structures containing V32I and L76M substitutions reveals a cooperative mechanism leading to structural deformation of flap-residue 45 that can modify PR2 flexibility | Human immunodeficiency virus 1 |
Q7K | naturally occuring mutation | Human immunodeficiency virus 1 |
V32I | site-directed mutagenesis, mutant enzyme structure modelling | Human immunodeficiency virus 1 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | 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. Modelling of PR1 mutant structures containing V32I and L76M substitutions reveals a cooperative mechanism leading to structural deformation of flap-residue 45 that can modify PR2 flexibility. Substitutions in the PR1 and PR2 pockets can modify PI binding and flap flexibility, which might underlie PR2 resistance against PIs | Human immunodeficiency virus 1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | P04587 | Gag-Pol polyprotein; HIV-1 | - |
Synonyms | Comment | Organism |
---|---|---|
HIV-2 protease | - |
Human immunodeficiency virus 1 |
PR2 | - |
Human immunodeficiency virus 1 |
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 1 |
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 1 |