The crystal structure analysis of the relative binding of cisplatin and carboplatin in a mixture with histidine in a protein studied at 100 and 300 K with repeated X-ray irradiation

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The crystal structure analysis of the relative binding of cisplatin and carboplatin in a mixture with histidine in a protein studied at 100 and 300 K with repeated X-ray irradiation

机译：晶体结构分析的相对的绑定顺铂和卡铂的混合物在100年,与组氨酸蛋白研究300 K与重复的x射线辐射

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The anticancer agents cisplatin and carboplatin bind to histidine in a protein. This crystal structure study at data-collection temperatures of 100 and 300 K examines their relative binding affinities to a histidine side chain and the effect of a high X-ray radiation dose of up to 1.8 MGy on the stability of the subsequent protein-Pt adducts. Cisplatin binding is visible at the histidine residue, but carboplatin binding is not. Five refined X-ray crystal structures are presented: one at 100 K as a reference and four at 300 K. The diffraction resolutions are 1.8, 2.0, 2.8, 2.9 and 3.5 ?.

机译：抗癌药物顺铂和卡铂绑定到组氨酸蛋白。结构研究收集温度100和300 K的检查他们的相对绑定组氨酸侧链和亲和力高的x射线辐射剂量的影响1.8 MGy随后的稳定性protein-Pt加合物。组氨酸残基,但卡铂绑定不是。介绍:一个在100 K作为参考和四个在300 K。2.0, 2.8, 2.9和3.5 ?。

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《Acta crystallographica.Section D. Biological crystallography》 |2013年第1期|121-125|共5页
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正文语种英语
中图分类化学;
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Histidine; structured analysis; crystal structureProteinCisplatinx ray irradiation;

机译：组氨酸、结构化分析、晶体structureProteinCisplatinx射线照射;

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The crystal structure analysis of the relative binding of cisplatin and carboplatin in a mixture with histidine in a protein studied at 100 and 300 K with repeated X-ray irradiation

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