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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data
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Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data

机译：还有从杜氏利什曼虫的结构一定会在2.6一项决议:环孢菌素关系结构和热力学数据

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摘要

Drug development against Leishmania donovani, the pathogen that causes visceral leishmaniasis in humans, is currently an active area of research given the widespread prevalence of the disease and the emergence of resistant strains. The immunosuppressive drug cyclosporin is known to have anti-parasitic activity against a variety of pathogens. The receptor for cyclosporin is the protein cyclophilin, which is a ubiquitous peptidylprolyl isomerase. The crystal structure of cyclophilin from L. donovani complexed with cyclosporin has been solved at 2.6 A resolution. The thermodynamic parameters of the interaction have been determined using spectroscopic and calorimetric techniques. A detailed effort has been made to predict the thermodynamic parameters of binding from computations based on the three-dimensional crystal structure. These results were in good agreement with the corresponding experimental values. Furthermore, the structural and biophysical results have been discussed in the context of leishmanial drug resistance and could also set the stage for the design of potent non-immunosuppressive antileishmanials.
机译：对杜氏利什曼虫的药物开发,导致内脏利什曼病的病原体人类,目前是一个活跃的研究领域考虑到广泛的疾病的发病率和耐药菌株的出现。免疫抑制剂环孢菌素是已知的寄生虫对各种活动吗病原体。还有蛋白质,这是一个无处不在peptidylprolyl异构酶。还有从l . donovani包裹着环孢菌素2.6决议已经解决了。相互作用的热力学参数已经决定使用光谱和量热技术。预测的热力学参数从计算基于绑定三维晶体结构。结果是在良好的协议相应的实验值。结构和生物物理结果的上下文中讨论了利什曼原虫的药物阻力,也可以设置的阶段设计有效的non-immunosuppressiveantileishmanials .

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