Human immunodeficiency virus type 1 aspartyl protease (HIV-1 protease (HIV-1 PR))

Human immunodeficiency virus type 1 aspartyl protease is a homodimeric enzyme essential for the life cycle and infectivity of HIV‑1. It catalyzes hydrolysis at specific sites within newly synthesized Gag and Gag–Pol polyproteins, producing mature structural proteins and enzymes required for assembly of infectious virions. The active site contains two catalytic Asp25 residues—one from each monomer—characteristic of aspartic proteases. Inhibiting this enzyme blocks production of mature virions, making it a critical therapeutic target in antiretroviral therapy against AIDS.

Other names

HIV-1 PRRetroviral aspartyl proteaseHIV retropepsinHuman immunodeficiency virus type 1 proteinase

Drugs targeting this molecule act as protease inhibitors. They bind to the active site of HIV‑1 protease, blocking its ability to cleave viral polyproteins. This prevents maturation of infectious virions, resulting in non-infectious viral particles.