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Science 30 July 2004:
Vol. 305. no. 5684, p. 569
DOI: 10.1126/science.305.5684.569n
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Isoforms of cytochrome P450 (CYP) are responsible for the oxidative metabolism of more than 90% of drugs in humans, and one isoform, CYP 3A4, is responsible for over 50% of hepatic drug metabolism. Now Williams et al. (p. 683, published online 15 July 2004) have determined the crystal structures of CYP 3A4, bound to either a substrate, to an inhibitor, or unliganded. The structures show very little change either on substrate or inhibitor binding. The substrate is bound in a peripheral binding site that may be involved in initial substrate binding or in binding to allosteric effectors. Conformational changes may be required for movement of substrate to the active site.




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Science. ISSN 0036-8075 (print), 1095-9203 (online)