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| {{STRUCTURE_1jrp| PDB=1jrp | SCENE= }} | | {{STRUCTURE_1jrp| PDB=1jrp | SCENE= }} |
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| '''Crystal Structure of Xanthine Dehydrogenase inhibited by alloxanthine from Rhodobacter capsulatus'''
| | ===Crystal Structure of Xanthine Dehydrogenase inhibited by alloxanthine from Rhodobacter capsulatus=== |
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| ==Overview==
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| Xanthine dehydrogenase (XDH), a complex molybdo/iron-sulfur/flavoprotein, catalyzes the oxidation of hypoxanthine to xanthine followed by oxidation of xanthine to uric acid with concomitant reduction of NAD+. The 2.7 A resolution structure of Rhodobacter capsulatus XDH reveals that the bacterial and bovine XDH have highly similar folds despite differences in subunit composition. The NAD+ binding pocket of the bacterial XDH resembles that of the dehydrogenase form of the bovine enzyme rather than that of the oxidase form, which reduces O(2) instead of NAD+. The drug allopurinol is used to treat XDH-catalyzed uric acid build-up occurring in gout or during cancer chemotherapy. As a hypoxanthine analog, it is oxidized to alloxanthine, which cannot be further oxidized but acts as a tight binding inhibitor of XDH. The 3.0 A resolution structure of the XDH-alloxanthine complex shows direct coordination of alloxanthine to the molybdenum via a nitrogen atom. These results provide a starting point for the rational design of new XDH inhibitors.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11796116}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11796116 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11796116}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Xdh]] | | [[Category: Xdh]] |
| [[Category: Xo]] | | [[Category: Xo]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:46:24 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:42:07 2008'' |