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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Towards investigation of the inhibitor-recognition mechanisms of drug-target proteins by neutron crystallography.
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Towards investigation of the inhibitor-recognition mechanisms of drug-target proteins by neutron crystallography.

机译:对inhibitor-recognition的调查机制的药物靶蛋白中子晶体学。

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摘要

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.
机译:通常知道酶代表重要的药物靶蛋白。和催化功能酶的分子识别机制提供了重要的信息基于结构的药物设计。晶体学提供准确的信息H原子的位置是至关重要的酶的功能和分子识别。最近的例子描述的结构测定药物靶蛋白的人类免疫缺陷病毒蛋白酶和猪胰弹性蛋白酶在复杂过渡态类似物抑制剂使用中子衍射仪生物晶体学(BIX-3和BIX-4)安装JRR-3研究反应堆。

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