Back بروتياز فيروس نقص المناعة البشرية-1 Arabic HIV-1 proteáza Czech HIV-Protease German Proteasa HIV 1 Spanish پروتئاز اچآیوی Persian HIV-1 protease ID HIV-1プロテアーゼ Japanese Proteaza HIV-1 Polish Протеаза ВИЧ-1 Russian HIV-1 retropepsin Serbo-Croatian
| HIV-1 Protease (Retropepsin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 HIV-1 protease dimer in white and grey, with peptide substrate in black and active site aspartate side chains in red. (PDB: 1KJF) | |||||||||
| Identifiers | |||||||||
| EC no. | 3.4.23.16 | ||||||||
| CAS no. | 144114-21-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
HIV-1 protease or PR is a retroviral aspartyl protease (retropepsin), an enzyme involved with peptide bond hydrolysis in retroviruses, that is essential for the life-cycle of HIV, the retrovirus that causes AIDS.[1][2] HIV-1 PR cleaves newly synthesized polyproteins (namely, Gag and Gag-Pol[3]) at nine cleavage sites to create the mature protein components of an HIV virion, the infectious form of a virus outside of the host cell.[4] Without effective HIV-1 PR, HIV virions remain uninfectious.[5][6]
- ^ Davies DR (1990). "The structure and function of the aspartic proteinases". Annual Review of Biophysics and Biophysical Chemistry. 19 (1): 189–215. doi:10.1146/annurev.bb.19.060190.001201. PMID 2194475.
- ^ Brik A, Wong CH (January 2003). "HIV-1 protease: mechanism and drug discovery". Organic & Biomolecular Chemistry. 1 (1): 5–14. doi:10.1039/b208248a. PMID 12929379.
- ^ Huang X, Britto MD, Kear-Scott JL, Boone CD, Rocca JR, Simmerling C, Mckenna R, Bieri M, Gooley PR, Dunn BM, Fanucci GE (June 2014). "The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics". The Journal of Biological Chemistry. 289 (24): 17203–14. doi:10.1074/jbc.M114.571836. PMC 4059161. PMID 24742668.
- ^ Lv Z, Chu Y, Wang Y (April 2015). "HIV protease inhibitors: a review of molecular selectivity and toxicity". HIV/AIDS: Research and Palliative Care. 7: 95–104. doi:10.2147/hiv.s79956. PMC 4396582. PMID 25897264.
- ^ Kräusslich HG, Ingraham RH, Skoog MT, Wimmer E, Pallai PV, Carter CA (February 1989). "Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides". Proceedings of the National Academy of Sciences of the United States of America. 86 (3): 807–11. Bibcode:1989PNAS...86..807K. doi:10.1073/pnas.86.3.807. PMC 286566. PMID 2644644.
- ^ Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RA, Scolnick EM, Sigal IS (July 1988). "Active human immunodeficiency virus protease is required for viral infectivity". Proceedings of the National Academy of Sciences of the United States of America. 85 (13): 4686–90. Bibcode:1988PNAS...85.4686K. doi:10.1073/pnas.85.13.4686. PMC 280500. PMID 3290901.