Structure of human cytidine deaminase bound to a potent inhibitor
Structure of human cytidine deaminase bound to a potent inhibitor
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DOI：
10.1021/jm0496279
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发表时间：
2005-02-10
影响因子：
7.3
通讯作者：
Verdine, GL
中科院分区：
文献类型：
--
作者：
Chung, SJ;Fromme, JC;Verdine, GL
人胞苷脱氨酶（CDA）是一种在催化核苷类抗癌和抗病毒剂代谢过程中发挥重要作用的酶。因此，它是开发小分子治疗佐剂的有前景的靶标。我们报告的第一个晶体结构的人CDA作为一个复杂的紧密结合的抑制剂，二氮杂卓酮核苷1。该结构揭示了抑制剂1能够与关键活性位点残基Phe 137建立典型的pi/pi相互作用。
Human cytidine deaminase (CDA) is an enzyme prominent for its role in catalyzing metabolic processing of nucleoside-type anticancer and antiviral agents. It is thus a promising target for the development of small molecule therapeutic adjuvants. We report the first crystal structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to establish a canonical pi/pi-interaction with a key active site residue, Phe 137.