1MUI

Crystal structure of HIV-1 protease complexed with Lopinavir.

Summary for 1MUI

• Entry DOI: 10.2210/pdb1mui/pdb
• Descriptor: protease, N-{1-BENZYL-4-[2-(2,6-DIMETHYL-PHENOXY)-ACETYLAMINO]-3-HYDROXY-5-PHENYL-PENTYL}-3-METHYL-2-(2-OXO-TETRAHYDRO-PYRIMIDIN-1-YL)-BUTYRAMIDE (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 2
• Total formula weight: 22236.31

Authors

Stoll, V.,Qin, W.,Stewart, K.D.,Jakob, C.,Park, C.,Walter, K.,Simmer, R.L.,Helfrich, R.,Bussiere, D.,Kao, J.,Kempf, D.,Sham, H.L.,Norbeck, D.W. (deposition date: 2002-09-23, release date: 2002-10-23, Last modification date: 2024-02-14)

Primary citation

Stoll, V.,Qin, W.,Stewart, K.D.,Jakob, C.,Park, C.,Walter, K.,Simmer, R.L.,Helfrich, R.,Bussiere, D.,Kao, J.,Kempf, D.,Sham, H.L.,Norbeck, D.W.
X-ray Crystallographic Structure of ABT-378 (Lopinavir) Bound to HIV-1 Protease
BIOORG.MED.CHEM., 10:2803-2806, 2002

PubMed Abstract: The crystal structure of ABT-378 (lopinavir), bound to the active site of HIV-1 protease is described. A comparison with crystal structures of ritonavir, A-78791, and BILA-2450 shows some analogous features with previous reported compounds. A cyclic urea unit in the P(2) position of ABT-378 is novel and makes two bidentate hydrogen bonds with Asp 29 of HIV-1 protease. In addition, a previously unreported shift in the Gly 48 carbonyl position is observed. A discussion of the structural features responsible for its high potency against wild-type HIV protease is given along with an analysis of the effect of active site mutations on potency in in vitro assays.

PubMed: 12057670
DOI: 10.1016/S0968-0896(02)00051-2

Experimental method

X-RAY DIFFRACTION (2.8 Å)