9HVP

Design, activity and 2.8 Angstroms crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease

Summary for 9HVP

• Entry DOI: 10.2210/pdb9hvp/pdb
• Related PRD ID: PRD_000256
• Descriptor: HIV-1 Protease, benzyl [(1R,4S,6S,9R)-4,6-dibenzyl-5-hydroxy-1,9-bis(1-methylethyl)-2,8,11-trioxo-13-phenyl-12-oxa-3,7,10-triazatridec-1-yl]carbamate (3 entities in total)
• Functional Keywords: acid proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 2
• Total formula weight: 22398.46

Authors

Neidhart, D.J.,Erickson, J. (deposition date: 1990-11-06, release date: 1992-04-15, Last modification date: 2024-02-14)

Primary citation

Erickson, J.,Neidhart, D.J.,VanDrie, J.,Kempf, D.J.,Wang, X.C.,Norbeck, D.W.,Plattner, J.J.,Rittenhouse, J.W.,Turon, M.,Wideburg, N.
Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease.
Science, 249:527-533, 1990

PubMed Abstract: 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.

PubMed: 2200122

Experimental method

X-RAY DIFFRACTION (2.8 Å)