Design, Activity, and 2.8 Å Crystal Structure of a C2 Symmetric Inhibitor Complexed to HIV-1 Protease
J Erickson, DJ Neidhart, J VanDrie, DJ Kempf… - Science, 1990 - science.org
J Erickson, DJ Neidhart, J VanDrie, DJ Kempf, XC Wang, DW Norbeck, JJ Plattner…
Science, 1990•science.orgA two-fold (C 2) symmetric inhibitor of the protease of human immunodeficiency virus type-1
(HIV-1) has been designed on the basis of the three-dimensional symmetry of the enzyme
active site. The symmetric molecule inhibited both protease activity and acute HIV-1 infection
in vitro, was at least 10,000-fold more potent against HIV-1 protease than against related
enzymes, and appeared to be stable to degradative enzymes. The 2.8 angstrom crystal
structure of the inhibitor-enzyme complex demonstrated that the inhibitor binds to the …
(HIV-1) has been designed on the basis of the three-dimensional symmetry of the enzyme
active site. The symmetric molecule inhibited both protease activity and acute HIV-1 infection
in vitro, was at least 10,000-fold more potent against HIV-1 protease than against related
enzymes, and appeared to be stable to degradative enzymes. The 2.8 angstrom crystal
structure of the inhibitor-enzyme complex demonstrated that the inhibitor binds to the …
A two-fold (C2) symmetric inhibitor of the protease of human immunodeficiency virus type-1 (HIV-1) has been designed on the basis of the three-dimensional symmetry of the enzyme active site. The symmetric molecule inhibited both protease activity and acute HIV-1 infection in vitro, was at least 10,000-fold more potent against HIV-1 protease than against related enzymes, and appeared to be stable to degradative enzymes. The 2.8 angstrom crystal structure of the inhibitor-enzyme complex demonstrated that the inhibitor binds to the enzyme in a highly symmetric fashion.
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