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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 Lewis,  
 

Homology modelling of human cytochromes P450 involved in xenobiotic metabolism and rationalization of substrate selectivity.

Molecular modelling of human cytochrome P450 ( CYP) isoforms is described, based on amino acid sequence homology with a unique bacterial P450 (CYP102) of known crystal structure. It is found that for the human hepatic P450s involved in the metabolism of xenobiotics, ie. CYPIA2, CYP 1A6, CYP2B6, CYP2C9, CYP2C 19, CYP2D6, CYP2E1 and CYP3A4, there is a satisfactory agreement between specific substrate characteristics and topographical features of the putative active sites, including complementarity with key amino acid residues in the P450 haem environments. A combination of homology model interactions with substrates and certain molecular properties of the compounds themselves provides a methodology for the evaluation of potential P450 selectivity in new chemical entities (NCEs).[1]

References

  1. Homology modelling of human cytochromes P450 involved in xenobiotic metabolism and rationalization of substrate selectivity. Lewis, D.F. Experimental and toxicologic pathology : official journal of the Gesellschaft für Toxikologische Pathologie. (1999) [Pubmed]
 
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