Modelling species selectivity in rat and human cytochrome P450 2D enzymes.
Edmund, GH, Lewis, DF and Howlin, BJ (2013) Modelling species selectivity in rat and human cytochrome P450 2D enzymes. PLoS One, 8 (5).
Available under License : See the attached licence file.
Updated models of the Rat Cytochrome P450 2D enzymes are produced based on the recent x-ray structures of the Human P450 2D6 enzyme both with and without a ligand bound. The differences in species selectivity between the epimers quinine and quinidine are rationalised using these models and the results are discussed with regard to previous studies. A close approach to the heme is not observed in this study. The x-ray structure of the enzyme with a ligand bound is shown to be a better model for explaining the observed experimental binding of quinine and quinidine. Hence models with larger closed binding sites are recommended for comparative docking studies. This is consistent with molecular recognition in Cytochrome P450 enzymes being the result of a number of non-specific interactions in a large binding site.
|Divisions :||Faculty of Engineering and Physical Sciences > Chemistry|
|Identification Number :||10.1371/journal.pone.0063335|
|Related URLs :|
|Additional Information :||Copyright 2013 Edmund et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.|
|Depositing User :||Symplectic Elements|
|Date Deposited :||10 Jul 2013 12:32|
|Last Modified :||09 Jun 2014 13:48|
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