1h69: Difference between revisions
New page: left|200px<br /> <applet load="1h69" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h69, resolution 1.86Å" /> '''CRYSTAL STRUCTURE O... |
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==About this Structure== | ==About this Structure== | ||
1H69 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FAD and ARH as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.2 1.6.99.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H69 OCA]]. | 1H69 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FAD and ARH as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Transferred_entry:_1.6.5.2 Transferred entry: 1.6.5.2]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.2 1.6.99.2]]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7 and AC8. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H69 OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Transferred entry: 1.6.5.2]] | |||
[[Category: Amzel, L.M.]] | [[Category: Amzel, L.M.]] | ||
[[Category: Bianchet, M.A.]] | [[Category: Bianchet, M.A.]] | ||
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[[Category: rossman fold]] | [[Category: rossman fold]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:31:57 2007'' | ||
Revision as of 12:27, 30 October 2007
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CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,3,5,6,TETRAMETHYL-P-BENZOQUINONE (DUROQUINONE) AT 2.5 ANGSTROM RESOLUTION
OverviewOverview
BACKGROUND: NAD(P)H:quinone acceptor oxidoreductase (QR1) protects animal, cells from the deleterious and carcinogenic effects of quinones and other, electrophiles. Remarkably, the same enzyme activates cancer prodrugs that, become cytotoxic only after two-electron reduction. QR1's ability to, bioactivate quinones and its elevated expression in many human solid, tumors makes this protein an excellent target for enzyme-directed drug, development. Until now, structural analysis of the mode of binding of, chemotherapeutic compounds to QR1 was based on model building using the, structures of complexes with simple substrates; no structure of complexes, of QR1 with chemotherapeutic prodrugs had been reported. RESULTS: Here we, report the high-resolution crystal structures of complexes of QR1 ... [(full description)]
About this StructureAbout this Structure
1H69 is a [Single protein] structure of sequence from [Homo sapiens] with FAD and ARH as [ligands]. Active as [Transferred entry: 1.6.5.2], with EC number [1.6.99.2]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7 and AC8. Full crystallographic information is available from [OCA].
ReferenceReference
Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones., Faig M, Bianchet MA, Winski S, Hargreaves R, Moody CJ, Hudnott AR, Ross D, Amzel LM, Structure. 2001 Aug;9(8):659-67. PMID:11587640
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