The ATP-binding site of type II topoisomerases as a target for antibacterial drugs

被引：230

作者：

Maxwell, A ^{[1
]}

Lawson, DM ^{[1
]}

机构：

[1] John Innes Ctr, Dept Biol Chem, Norwich NR4 7UH, Norfolk, England

来源：

CURRENT TOPICS IN MEDICINAL CHEMISTRY | 2003年 / 3卷 / 03期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.2174/1568026033452500

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

DNA topoisomerases are essential enzymes in all cell types and have been found to be valuable drug targets both for antibacterial and anti-cancer chemotherapy. Type II topoisomerases possess a binding site for ATP, which can be exploited as a target for chemo-therapeutic agents. High-resolution structures of protein fragments containing this site complexed with antibiotics or an ATP analogue have provided vital information for the understanding of the action of existing drugs and for the potential development of novel anti-bacterial agents. In this article we have reviewed the structure and function of the ATPase domain of DNA gyrase (bacterial topoisomerase II), particularly highlighting novel information that has been revealed by structural studies. We discuss the efficacy and mode of action of existing drugs and consider the prospects for the development of novel agents.

引用

页码：283 / 303

页数：21

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