Nature 337, 615 - 620 (16 February 1989); doi:10.1038/337615a0

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

Manuel A. Navia^*, Paula M. D. Fitzgerald^*, Brian M. McKeever^*, Chih-Tai Leu^†, Jill C. Heimbach^†, Wayne K. Herber^†, Irving S. Sigal^†‡, Paul L. Darke^† & James P. Springer^*

^*Department of Biophysical Chemistry, Merck Sharp and Dohme Research Laboratories, PO Box 2000 (RY80M-203), Rahway, New Jersey 07065, USA
^†Department of Molecular Biology, Merck Sharp and Dohme Research Laboratories, Sumneytown Pike (WP16-101), West Point, Pennsylvania 19486, USA
^‡Sadly, Dr Irving S. Sigal was killed in the destruction of Pan Am Flight 103 over Lockerbie, Scotland on 20 December 1988.

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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