Literature summary 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 .
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.4.23.47 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.23.47 |
Human immunodeficiency virus 2 |
P04584 |
Gag-Pol polyprotein; HIV-2 |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.23.47 |
additional information |
PR2 recognizes various non-homologous substrates (Gag and Pol polyproteins) at several cleavage sites and protease inhibitors |
Human immunodeficiency virus 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 |
- |
Human immunodeficiency virus 2 |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.4.23.47 |
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 |
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 |
Human immunodeficiency virus 2 |