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

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

P A Williams  1 , J Cosme, V Sridhar, E F Johnson, D E McRee
Affiliations

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

P A Williams et al. J Inorg Biochem. .

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.

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