EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.4.23.47 | I32V | site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16). The mutation increases the susceptibility of HIV-2 to multiple protease inhibitors | Human immunodeficiency virus 2 |
3.4.23.47 | I82V | site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16) | Human immunodeficiency virus 2 |
3.4.23.47 | M76L | site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16). The mutation increases the susceptibility of HIV-2 to multiple protease inhibitors | Human immunodeficiency virus 2 |
3.4.23.47 | additional information | construction of HIV-2ROD9 molecular clones containing amino acid changes corresponding to wild-type HIV-1 amino acids (I32V, V47I, M76L, and I82V) either individually or together (clone PRDELTA4) and comparison of the phenotypic sensitivities (50% effective concentration [EC50]) of mutant and wild-type viruses to nine FDA-approved protease inhibitors, overview. Clone PRDELTA4 show protease inhibitor susceptibility equivalent to or greater than that of HIV-1 for all protease inhibitors | Human immunodeficiency virus 2 |
3.4.23.47 | V47I | site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16). The mutation increases the susceptibility of HIV-2 to multiple protease inhibitors | Human immunodeficiency virus 2 |
3.4.23.47 | V47I/M76L/I32V/I82V | site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16). The combination of the four amino acid changes in HIV-2 protease confers a pattern of protease inhibitor susceptibility comparable to that of HIV-1 | Human immunodeficiency virus 2 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.23.47 | darunavir | - |
Human immunodeficiency virus 2 | |
3.4.23.47 | lopinavir | - |
Human immunodeficiency virus 2 | |
3.4.23.47 | additional information | HIV-2 exhibits intrinsic resistance to most FDA-approved HIV-1 protease inhibitors, retaining clinically useful susceptibility only to lopinavir, darunavir, and saquinavir. Structural rationale for intrinsic HIV-2 PI resistance. No inhibition by amprenavir, atazanavir, indinavir, nelfinavir, ritonavir, and tipranavir. Phenotypic protease inhibitor sensitivities of wild-type HIV-1, wild-type HIV-2, and mutant HIV-2 strains, overview | Human immunodeficiency virus 2 | |
3.4.23.47 | saquinavir | - |
Human immunodeficiency virus 2 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.23.47 | Human immunodeficiency virus 2 | P04584 | Gag-Pol polyprotein; HIV-2 | - |
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 |