HIV-1 protease (PR) is a retroviral aspartyl protease (retropepsin), an enzyme involved with peptide bondhydrolysis in retroviruses, that is essential for the life-cycle of HIV, the retrovirus that causes AIDS.[1][2] HIV protease 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 protease, HIV virions remain uninfectious.[5][6]
| HIV-1 Protease (Retropepsin) | |
|---|---|
 HIV-1 protease dimer in white and grey, with peptide substrate in black and active siteaspartate 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 |
| PDBstructures | RCSB PDB PDBePDBsum |
| Gene Ontology | AmiGO / QuickGO |
The catalytic mechanism of a general aspartyl protease, containing the two characteristic Asp25 residues in the deprotonated and protonated forms. "Aspartyl proteae mechanism.png"
https://en.wikipedia.org/wiki/HIV-1_protease
https://meshb.nlm.nih.gov/record/ui?name=HIV-1%20Protease
http://merops.sanger.ac.uk
http://proteopedia.org/wiki/index.php/Main_Page
above.
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