Title of article
X-ray crystallographic structure of ABT-378 (Lopinavir) bound to HIV-1 protease Original Research Article
Author/Authors
Vincent Stoll، نويسنده , , Wenying Qin، نويسنده , , Kent D. Stewart، نويسنده , , Clarissa Jakob، نويسنده , , Chang Park، نويسنده , , K. Walter، نويسنده , , R.L. Simmer، نويسنده , , Rosalind Helfrich، نويسنده , , Dirk Bussiere، نويسنده , , J. Kao، نويسنده , , Dale Kempf، نويسنده , , Hing L. Sham، نويسنده , , Daniel W. Norbeck، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2002
Pages
4
From page
2803
To page
2806
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 P2 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.
Journal title
Bioorganic and Medicinal Chemistry
Serial Year
2002
Journal title
Bioorganic and Medicinal Chemistry
Record number
1302211
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