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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.
The function of HIV protease is to cleave the initial polyprotein into its functional constituents (Sussman et al., 2013). This enzyme is made up of a dimer of identical subunits that mimics the two-lobed monomeric structure of pepsin and other aspartate proteases.
The HIV-1 protease (HIV-1 PR) is a virus-specific aspartic protease responsible for processing the polyproteins of gag and gag-pol during virion maturation and for the proliferation of the retrovirus (Fig. 2.7).
HIV-1 protease, like human renin, is an aspartyl protease and functions as a C 2 symmetric homodimer, with each monomer consisting of 99 amino acids. One of its targets is the amide bond intervening the dipeptide sequence Phe/Tyr-Pro, which represents a unique cleavage sequence not shared by mammalian proteases and consequently represents an ...
HIV protease, the third virally encoded enzyme, is required in this step to cleave a viral polyprotein precursor into individual mature proteins. The viral RNA and viral proteins assemble at the cell surface into new virions, which then bud from the cell and are released to infect another cell.
HIV-1 protease performs an essential step in the life cycle of HIV. Like many viruses, HIV makes many of its proteins in one long piece, with several proteins strung together. HIV-1 protease has the job of cutting this long "polyprotein" into the proper protein-sized pieces.
HIV protease is responsible for processing of the gag and gag-pol polyproteins during virion maturation. The activity of this enzyme is essential for virus infectivity, rendering the protein a major therapeutic target for AIDS treatment. This articles reviews the biochemical and biophysical properti …
