Microsomal cytochrome P4502C5: comparison to microbial P450s and unique features

被引：104
|
作者：
Williams, PA
Cosme, J
Sridhar, V
Johnson, EF
McRee, DE
机构：
[1] Scripps Res Inst, Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Res Inst, Dept Mol & Expt Med, La Jolla, CA 92037 USA
来源：
JOURNAL OF INORGANIC BIOCHEMISTRY | 2000年 / 81卷 / 03期
关键词：
cytochrome P450; microsomal P450; crystal structure;
D O I：
10.1016/S0162-0134(00)00102-1
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2000 Elsevier Science S.A. All rights reserved.
引用
收藏
页码：183 / 190
页数：8
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