EC Number   |
General Information |
Reference |
|---|
   3.4.23.47 | evolution |
HIV proteases PR1 and PR2 share only approximately 50% of sequence identity but they exhibit a similar global fold |
755505 |
| 3.4.23.47 | more |
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 |
754210 |
| 3.4.23.47 | more |
comparison of the HIV-1 protease and HIV-2 protease binding pockets extracted from structures complexed with 12 ligands, overview |
755505 |
| 3.4.23.47 | more |
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 |
755507 |
| 3.4.23.47 | physiological function |
HIV PR2 is essential for hydrolysing the viral Gag and the Gag-Pol precursor polyproteins during the maturation of infectious viral particles |
755507 |
