1w0f: Difference between revisions

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[[Image:1w0f.~~gif~~|left|200px]]

[[Image:1w0f.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4~~'''~~

===CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4===

~~==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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==About this Structure==

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[[Category: Nifedipine oxidase]]

[[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 Sun Jul 27 20:12:10 2008''

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-[[Image:1w0f.gif|left|200px]]
+{{Seed}}
+[[Image:1w0f.png|left|200px]]
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 {{STRUCTURE_1w0f|  PDB=1w0f  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4'''
+===CRYSTAL STRUCTURE OF HUMAN CYTOCHROME P450 3A4===
-==Overview==
+<!--
-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.
+-->
+{{ABSTRACT_PUBMED_15256616}}
 ==About this Structure==
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 [[Category: Nifedipine oxidase]]
 [[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 Sun Jul 27 20:12:10 2008''