Taylor P, Page A P, Kontopidis G, Husi H, Walkinshaw M D
Structural Biochemistry Group, The University of Edinburgh, UK.
FEBS Lett. 1998 Mar 27;425(2):361-6. doi: 10.1016/s0014-5793(98)00264-6.
A structure of residues 1-177 of the cyclophilin domain of a large divergent cyclophilin from the filarial nematode parasite Brugia malayi has been crystallised and solved in two different crystal forms. The active site has a similar structure to that of human cyclophilin A. Two of the 13 residues important in forming the human cyclophilin A/cyclosporin A complex are altered in the B. malayi cyclophilin and explain the relatively poor inhibition of peptidyl prolyl isomerase activity by cyclosporin A.
来自丝虫线虫寄生虫马来布鲁线虫的一种高度分化的亲环蛋白的亲环蛋白结构域1-177位残基的结构已通过两种不同的晶体形式进行了结晶和解析。其活性位点与人类亲环蛋白A的结构相似。在形成人类亲环蛋白A/环孢菌素A复合物中起重要作用的13个残基中的两个在马来布鲁线虫亲环蛋白中发生了改变，这解释了环孢菌素A对肽基脯氨酰异构酶活性的抑制作用相对较弱的原因。
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