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Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1

Nature volume 337, pages 615–620 (1989)Cite this article

Abstract

The crystal structure of the protease of the human immunodeficiency virus type 1 (HIV-1), which releases structural proteins and enzymes from viral polyprotein products, has been determined to 3 Å resolution. Large regions of the protease dimer, including the active site, have structural homology to the family of microbial aspartyl proteases. The structure suggests a mechanism for the autoproteolytic release of protease and a role in the control of virus maturation.

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Authors and Affiliations

  1. Department of Biophysical Chemistry, Merck Sharp and Dohme Research Laboratories, PO Box 2000 (RY80M-203), Rahway, New Jersey, 07065, USA

    Manuel A. Navia, Paula M. D. Fitzgerald, Brian M. McKeever & James P. Springer

  2. Department of Molecular Biology, Merck Sharp and Dohme Research Laboratories, Sumneytown Pike (WP16-101), West Point, Pennsylvania, 19486, USA

    Chih-Tai Leu, Jill C. Heimbach, Wayne K. Herber, Irving S. Sigal & Paul L. Darke

Author notes

  1. Sadly, Dr Irving S. Sigal was killed in the destruction of Pan Am Flight 103 over Lockerbie, Scotland on 20 December 1988.

    • Irving S. Sigal
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  1. Manuel A. Navia
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Navia, M., Fitzgerald, P., McKeever, B. et al. Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1. Nature 337, 615–620 (1989). https://doi.org/10.1038/337615a0

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