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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution
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The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution

机译：鼠伤寒沙门氏菌的x射线结构尿苷核苷磷酸化酶包裹着2, 2’-anhydrouridine、磷和钾离子1.86一项决议

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摘要

Uridine nucleoside phosphorylase is an important drug target for the development of anti-infective and antitumour agents. The X-ray crystal structure of Salmonella typhimurium uridine nucleoside phosphorylase (StUPh) complexed with its inhibitor 2,2'-anhydrouridine, phosphate and potassium ions has been solved and refined at 1.86 A resolution (R_(cryst) = 17.6%, R_(free) = 20.6%). The complex of human uridine phosphorylase I (HUPhI) with 2,2'-anhydrouridine was modelled using a computational approach. The model allowed the identification of atomic groups in 2,2'-anhydrouridine that might improve the interaction of future inhibitors with StUPh and HUPhI.
机译：尿苷核苷磷酸化酶是一个重要的抗感染药物的目标发展和抗肿瘤剂。鼠伤寒沙门氏菌尿苷的结构核苷磷酸化酶(StUPh)包裹着其抑制剂2,2’-anhydrouridine、磷酸盐和钾离子已经解决和完善1.86一项决议(R_(结晶)= 17.6%,R_(免费)=20.6%)。磷酸化酶(HUPhI) 2、2’-anhydrouridine使用的计算方法是模仿。模型允许原子组的识别2, 2’-anhydrouridine可能改善相互作用的抑制剂StUPh和未来HUPhI。

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