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. 1989 Feb 17;243(4893):928-31.
doi: 10.1126/science.2537531.

Molecular modeling of the HIV-1 protease and its substrate binding site

I T Weber  1 , M Miller, M Jaskólski, J Leis, A M Skalka, A Wlodawer
Affiliations

Molecular modeling of the HIV-1 protease and its substrate binding site

I T Weber et al. Science. .

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.

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