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Science 17 February 1989:
Vol. 243. no. 4893, pp. 928 - 931
DOI: 10.1126/science.2537531
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Articles

Science, Vol 243, Issue 4893, 928-931
Copyright © 1989 by American Association for the Advancement of Science

articles

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

IT Weber, M Miller, M Jaskolski, J Leis, AM Skalka, and A Wlodawer

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.


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Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution.
M Miller, J Schneider, B. Sathyanarayana, M. Toth, G. Marshall, L Clawson, L Selk, S. Kent, and A Wlodawer (1989)
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NCI team remodels key AIDS virus enzyme.
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Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease.
A Wlodawer, M Miller, M Jaskolski, B. Sathyanarayana, E Baldwin, I. Weber, L. Selk, L Clawson, J Schneider, and S. Kent (1989)
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