Towards investigation of the inhibitorrecognition mechanisms of drug-target proteins by neutron crystallography.
Towards investigation of the inhibitorrecognition mechanisms of drug-target proteins by neutron crystallography.
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通过中子晶体学研究药物靶蛋白的抑制剂识别机制。
DOI：
10.1107/s0907444910034967
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Tamada T
中科院分区：
文献类型：
--
作者：
Kuroki R;Okazaki N;Adachi M;Ohhara T;Kurihara K;Tamada T
It is generally known that enzymes represent important drug-target proteins. Elucidation of the catalytic function and the molecular-recognition mechanisms of enzymes provides important information for structure-based drug design. Neutron crystallography provides accurate information on the locations of H atoms that are essential in enzymatic function and molecular recognition. Recent examples are described of the structure determination of the drug-target proteins human immunodeficiency virus protease and porcine pancreatic elastase in complex with transition-state analogue inhibitors using the neutron diffractometers for biological crystallography (BIX-3 and BIX-4) installed at the JRR-3 research reactor.
