From model complexes to metalloprotein inhibition: A synergistic approach to structure-based drug discovery

被引：29

作者：

Puerta, DT

Schames, JR

Henchman, RH

McCammon, JA

Cohen, SM

机构：

[1] Univ Calif San Diego, Howard Hughes Med Inst, Dept Chem & Biochem, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2003年 / 42卷 / 32期

关键词：

bioinorganic chemistry; computer chemistry; drug design; metalloproteins; zinc;

D O I：

10.1002/anie.200351433

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A happy marriage: The combination of synthetic model chemistry with computational conformational analysis has revealed the binding of an inhibitor to a medically important metalloenzyme. [(TpPh,Me)Zn(mbt)] (Tp Ph,Me = hydrotris (3,5-phenylmethylpyrazolyl)borate, mbt = 2-methoxybenzenethiol) was used to template the conformation of a known inhibitor in the active site of the metalloenzyme, as shown by the green ligand inside the active site of the protein (the Zn11 ion is shown in purple).

引用

页码：3772 / 3774

页数：3