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

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. © 1989 Nature Publishing Group.