Mechanism of Autoprocessing of a Mini-Precursor of the Aspartic Protease of Human Immunodeficiency Virus Type 1
Mechanism of Autoprocessing of a Mini-Precursor of the Aspartic Protease of Human Immunodeficiency Virus Type 1
During the expression of human immunodeficiency virus (HIV) genome to make new virions, the 99-residue protease monomer is synthesized as part of the Pr160 gag-pol precursor. After the virions are budded-out from the cell surface, the Pr160 gag-pol polyprotein is autoprocessed at eight different sites to produce mature gag proteins (p17, p24, p7, and p6) and 3 HIV enzymes (protease, reverse transcriptase, and integrase). The autoprocessing is essential for the assembly of the interior of HIV virion and is essential for the infectiousness of the virus.
- University of Oklahoma Health Sciences Center United States
- Oklahoma Medical Research Foundation United States
Enzyme Precursors, Protein Conformation, Molecular Sequence Data, Recombinant Proteins, Models, Structural, Kinetics, HIV Protease, Computer Graphics, HIV-1, Humans, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Cloning, Molecular, Protein Processing, Post-Translational
Enzyme Precursors, Protein Conformation, Molecular Sequence Data, Recombinant Proteins, Models, Structural, Kinetics, HIV Protease, Computer Graphics, HIV-1, Humans, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Cloning, Molecular, Protein Processing, Post-Translational
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