1og2: Difference between revisions
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[[Image:1og2.gif|left|200px]] | [[Image:1og2.gif|left|200px]] | ||
'''STRUCTURE OF HUMAN CYTOCHROME P450 CYP2C9''' | {{Structure | ||
|PDB= 1og2 |SIZE=350|CAPTION= <scene name='initialview01'>1og2</scene>, resolution 2.60Å | |||
|SITE= <scene name='pdbsite=HC1:Hec+Binding+Site+For+Chain+B'>HC1</scene> | |||
|LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF HUMAN CYTOCHROME P450 CYP2C9''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OG2 is a [ | 1OG2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OG2 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of human cytochrome P450 2C9 with bound warfarin., Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H, Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. PMID:[http:// | Crystal structure of human cytochrome P450 2C9 with bound warfarin., Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H, Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12861225 12861225] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:10:26 2008'' | ||
Revision as of 14:10, 20 March 2008
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| , resolution 2.60Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Unspecific monooxygenase, with EC number 1.14.14.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF HUMAN CYTOCHROME P450 CYP2C9
OverviewOverview
Cytochrome P450 proteins (CYP450s) are membrane-associated haem proteins that metabolize physiologically important compounds in many species of microorganisms, plants and animals. Mammalian CYP450s recognize and metabolize diverse xenobiotics such as drug molecules, environmental compounds and pollutants. Human CYP450 proteins CYP1A2, CYP2C9, CYP2C19, CYP2D6 and CYP3A4 are the major drug-metabolizing isoforms, and contribute to the oxidative metabolism of more than 90% of the drugs in current clinical use. Polymorphic variants have also been reported for some CYP450 isoforms, which has implications for the efficacy of drugs in individuals, and for the co-administration of drugs. The molecular basis of drug recognition by human CYP450s, however, has remained elusive. Here we describe the crystal structure of a human CYP450, CYP2C9, both unliganded and in complex with the anti-coagulant drug warfarin. The structure defines unanticipated interactions between CYP2C9 and warfarin, and reveals a new binding pocket. The binding mode of warfarin suggests that CYP2C9 may undergo an allosteric mechanism during its function. The newly discovered binding pocket also suggests that CYP2C9 may simultaneously accommodate multiple ligands during its biological function, and provides a possible molecular basis for understanding complex drug-drug interactions.
About this StructureAbout this Structure
1OG2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human cytochrome P450 2C9 with bound warfarin., Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H, Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. PMID:12861225
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