Molecular modeling of the HIV-1 protease and its substrate binding site.
The human immunodeficiency virus (HIV-1) encodes a protease that is essential for viral replication and is a member of the aspartic protease family. The recently determined three-dimensional structure of the related protease from Rous sarcoma virus has been used to model the smaller HIV-1 dimer. The active site has been analyzed by comparison to the structure of the aspartic protease, rhizopuspepsin, complexed with a peptide inhibitor. The HIV-1 protease is predicted to interact with seven residues of the protein substrate. This information can be used to design protease inhibitors and possible antiviral drugs.
Weber
I T
IT
Crystallography Laboratory, NCI-Frederick Cancer Research Facility, MD 21701.
Miller
M
M
Jaskólski
M
M
Leis
J
J
Skalka
A M
AM
Wlodawer
A
A
D000595:Amino Acid Sequence; D001358:Avian Sarcoma Viruses / Q000201:enzymology; D001665:Binding Sites; D015497:HIV-1 / Q000201:enzymology*; D006860:Hydrogen Bonding; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000378:metabolism*; D011487:Protein Conformation
D046911:Macromolecular Substances; D010447:Peptide Hydrolases