About this Biochemistry, Genetics and Molecular Biology article

A three-dimensional model of aromatase cytochrome P450 by Sandra Graham-Lorence; Julian A. Peterson; Bilal Amarneh; Evan R. Simpson; Ronald E. White is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

## Abstract P450 hemeproteins comprise a large gene superfamily that catalyzes monooxygenase reactions in the presence of a redox partner. Because the mammalian members are, without exception, membrane‐bound proteins, they have resisted structure‐function analysis by means of X‐ray crystallographic methods. Among P450‐catalyzed reactions, the aromatase reaction that catalyzes the conversion of C19 steroids to estrogens is one of the most complex and least understood. Thus, to better understand the reaction mechanism, we have constructed a three‐dimensional model of P450arom not only to examine the active site and those residues potentially involved in catalysis, but to study other important structural features such as substrate recognition and redox‐partner binding, which require examination of the entire molecule (excepting the putative membrane‐spanning region). This model of P450arom was built based on a “core structure” identified from the structures of the soluble, bacterial P450s (P450cam, P450terp, and P450BM‐P) rather than by molecular replacement, after which the less conserved elements and loops were added in a rational fashion. Minimization and dynamic simulations were u

Author

Sandra Graham-Lorence; Julian A. Peterson; Bilal Amarneh; Evan R. Simpson; Ronald E. White

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1995

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)