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Natasha M. DeVore, Kathleen M. Meneely, Aaron G. Bart, Eva S. Stephens, Kevin P. Battaile and Emily E. Scott Structural comparison of cytochromes P450 2A6, 2A13, and 2E1 with pilocarpine The FEBS Journal 279

Version of Record online: 25 NOV 2011 | DOI: 10.1111/j.1742-4658.2011.08412.x

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Human xenobiotic-metabolizing cytochrome P450 enzymes each bind and monooxygenate a diverse sets of drug substrates, but protein structural similarities and differences controlling overlapping selectivity are not well understood. Structures for three human cytochrome P450 enzymes (CYP2A6, CYP2A13, and CYP2A13) binding the common inhibitor pilocarpine, a muscarinic receptor agonist, reveal how individual amino acids result in different binding orientations.

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