Structure of human ACE gives new insights into inhibitor binding and design
Structure of human ACE gives new insights into inhibitor binding and design
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DOI：
10.1016/s0165-6147(03)00196-2
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发表时间：
2003-08-01
影响因子：
13.8
通讯作者：
Brew, K
中科院分区：
文献类型：
--
作者：
Brew, K
血管紧张素转换酶（ACE）是控制高血压药物的主要作用靶点。ACE关键催化结构域的新X射线晶体学结构提供了有关其位于深通道中的活性位点结构及其与抑制剂相互作用的详细信息。这些信息可能有助于ACE抑制剂的合理设计，更有效，更有选择性，因此临床使用。
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.