Investigating Human P450s Involved in Drug Metabolism via Homology with High-Resolution P450 Crystal Structures of the CYP2C Subfamily

Author(s): David F.V. Lewis, Yuko Ito, Peter S. Goldfarb

Journal Name: Current Drug Metabolism

Volume 7 , Issue 6 , 2006

Become EABM
Become Reviewer
Call for Editor


The important role of high-resolution crystal structures of cytochrome P450 (CYP) enzymes for the generation of P450 models by homology is discussed. The main focus is on human P450 enzymes involved in drug metabolism, where the role of homology modelling has been emphasized in the recent literature. Report of the first human P450 crystal structure has provided an opportunity for comparison between those modelled from other crystallographic templates, and the recent substrate-bound rabbit CYP2C5 structure exemplifies the relevance of high-resolution template structures to generating 3-D models of P450s where the homology is relatively high. In particular, the homology models of human CYP1 and CYP2 family enzymes are presented, where good agreement with experiment findings are apparent.

Keywords: Cytochromes P450, Human Drug Metabolism, Structural Modeling

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2006
Page: [589 - 598]
Pages: 10
DOI: 10.2174/138920006778017812
Price: $65

Article Metrics

PDF: 4