Human immunodeficiency virus (HIV) protease, belonging to the aspartic proteinase family, is an enzyme encoded by the pol open reading frame (ORF) of HIV genome that catalyze the posttranslational processing of the HIV polyproteins to yield structural proteins of the viral core and enzymes. The chemical structure of a HIV protease molecule is a symmetrical homodimer in which the interface is formed primarily by a four-stranded antiparallel β-sheet. A conserved D25-T26-G27 triad has been identified in each HIV protease monomer, which is positioned in a loop forming part of the catalytic site. HIV protease has been found to cleave peptide bonds in the p55 gag and p160 gag-pol polyproteins as well as in various cellular proteins in vitro, including calmodulin, pro-interleukin 1β and NF-KB.
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