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Comparative Study
. 1989 Feb 16;337(6208):615-20.
doi: 10.1038/337615a0.

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

M A Navia  1 , P M Fitzgerald, B M McKeever, C T Leu, J C Heimbach, W K Herber, I S Sigal, P L Darke, J P Springer
Affiliations
Comparative Study

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

M A Navia et al. Nature. .

Abstract

The crystal structure of the protease of the human immunodeficiency virus type (HIV-1), which releases structural proteins and enzymes from viral polyprotein products, has been determined to 3 A 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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