| Literature DB >> 2537531 |
I T Weber1, M Miller, M Jaskólski, J Leis, A M Skalka, A Wlodawer.
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.Entities:
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Year: 1989 PMID： 2537531 DOI： 10.1126/science.2537531
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728