Structure of human ACE gives new insights into inhibitor binding and design

被引：26

作者：

Brew, K ^{[1
]}

机构：

[1] Florida Atlantic Univ, Dept Biomed Sci, Boca Raton, FL 33431 USA

来源：

TRENDS IN PHARMACOLOGICAL SCIENCES | 2003年 / 24卷 / 08期

关键词：

D O I：

10.1016/S0165-6147(03)00196-2

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Angiotensin-converting enzyme (ACE) is a primary target of drugs used for controlling hypertension. A new X-ray crystallographic structure of the key catalytic domain of ACE provides detailed information about the structure of its active site, located in a deep channel, and its interactions with an inhibitor. Such information might facilitate the rational design of ACE inhibitors that are more potent and more selective and therefore of clinical use.

引用

页码：391 / 394

页数：4

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