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X-ray crystallographic structure of ABT-378 (Lopinavir) bound to HIV-1 protease
Vincent Stoll ,
Wenying Qin ,
Kent D. Stewart ,
Clarissa Jakob ,
Chang Park ,
K. Walter ,
R.L. Simmer ,
Rosalind Helfrich ,
Dirk Bussiere ,
J. Kao ,
Dale Kempf ,
Hing L. Sham ,
Daniel W. Norbeck
August 2002
August 2002
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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.