Structural highlights
Publication Abstract from PubMed
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.
Molecular modeling of the HIV-1 protease and its substrate binding site.,Weber IT, Miller M, Jaskolski M, Leis J, Skalka AM, Wlodawer A Science. 1989 Feb 17;243(4893):928-31. PMID:2537531[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Weber IT, Miller M, Jaskolski M, Leis J, Skalka AM, Wlodawer A. Molecular modeling of the HIV-1 protease and its substrate binding site. Science. 1989 Feb 17;243(4893):928-31. PMID:2537531
