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X-ray crystallographic structure of ABT-378 (lopinavir) bound to HIV-1 protease.

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.

journal_name

Bioorg Med Chem

journal_title

Bioorganic & medicinal chemistry

authors

Stoll V,Qin W,Stewart KD,Jakob C,Park C,Walter K,Simmer RL,Helfrich R,Bussiere D,Kao J,Kempf D,Sham HL,Norbeck DW

doi

10.1016/s0968-0896(02)00051-2

subject

Has Abstract

pub_date

2002-08-01 00:00:00

pages

2803-6

issue

8

eissn

0968-0896

issn

1464-3391

pii

S0968089602000512

journal_volume

10

pub_type

杂志文章

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