Display Settings:

Format

Send to:

Choose Destination

    Science. 1989 Feb 17;243(4893):928-31.

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

    Weber IT, Miller M, Jaskólski M, Leis J, Skalka AM, Wlodawer A.

    Crystallography Laboratory, NCI-Frederick Cancer Research Facility, MD 21701.

    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.

    PMID: 2537531 [PubMed - indexed for MEDLINE]

    Supplemental Content

    Click here to read

    Structures reported by this article