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| {{STRUCTURE_1w0g| PDB=1w0g | SCENE= }} | | {{STRUCTURE_1w0g| PDB=1w0g | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4'''
| | ===CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4=== |
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| ==Overview==
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| Cytochromes P450 (P450s) metabolize a wide range of endogenous compounds and xenobiotics, such as pollutants, environmental compounds, and drug molecules. The microsomal, membrane-associated, P450 isoforms CYP3A4, CYP2D6, CYP2C9, CYP2C19, CYP2E1, and CYP1A2 are responsible for the oxidative metabolism of more than 90% of marketed drugs. Cytochrome P450 3A4 (CYP3A4) metabolizes more drug molecules than all other isoforms combined. Here we report three crystal structures of CYP3A4: unliganded, bound to the inhibitor metyrapone, and bound to the substrate progesterone. The structures revealed a surprisingly small active site, with little conformational change associated with the binding of either compound. An unexpected peripheral binding site is identified, located above a phenylalanine cluster, which may be involved in the initial recognition of substrates or allosteric effectors.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15256616}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15256616 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15256616}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nifedipine oxidase]] | | [[Category: Nifedipine oxidase]] |
| [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:59:21 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:21:20 2008'' |