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微粒体细胞色素P450 2C5:与微生物P450的比较及独特特征

Microsomal cytochrome P450 2C5: comparison to microbial P450s and unique features.

作者信息

Williams P A, Cosme J, Sridhar V, Johnson E F, McRee D E

机构信息

Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

出版信息

J Inorg Biochem. 2000 Aug 31;81(3):183-90. doi: 10.1016/s0162-0134(00)00102-1.

Abstract

Although microsomal P450s represent the majority of P450s, only microbial P450s have been amenable to crystal structure solution. We have recently solved the first crystal structure of a microsomal P450, 2C5, a progesterone hydroxylase from rabbit. We discuss the features of the protein in common with existing structures of microbial P450s and limitations of homology modeling mammalian P450s based on the microbial structures. Unique features involving membrane, substrate and cytochrome P450 reductase interactions are also discussed.

摘要

尽管微粒体细胞色素P450占细胞色素P450的大多数,但只有微生物细胞色素P450适合进行晶体结构解析。我们最近解析了微粒体细胞色素P450 2C5(一种来自兔子的孕酮羟化酶)的首个晶体结构。我们讨论了该蛋白质与微生物细胞色素P450现有结构共有的特征,以及基于微生物结构对哺乳动物细胞色素P450进行同源建模的局限性。还讨论了涉及膜、底物和细胞色素P450还原酶相互作用的独特特征。

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