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

Irene T. Weber*, Maria Miller, Mariusz Jaskólski, Jonathan Leis, Anna Marie Skalka, Alexander Wlodawer

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

131 Scopus citations

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 ofthe protein substrate. This information can be used to design protease inhibitors and possible antivirual drugs.

Original languageEnglish (US)
Pages (from-to)928-931
Number of pages4
JournalScience
Volume243
Issue number4893
DOIs
StatePublished - 1989

ASJC Scopus subject areas

  • General

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