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Molecular modeling of the HIV-1 protease and its substrate binding site
I T Weber1, M Miller, M Jaskólski
1Crystallography Laboratory, NCI-Frederick Cancer Research Facility, MD 21701.
Science (New York, N.Y.)
|February 17, 1989
Abstract:
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.