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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Avian Sarcoma Viruses / enzymology
  • Binding Sites
  • HIV-1 / enzymology*
  • Hydrogen Bonding
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Hydrolases / metabolism*
  • Protein Conformation

Substances

  • Macromolecular Substances
  • Peptide Hydrolases