https://proteopedia.org/index.php?action=history&feed=atom&title=NADH_quinone_oxidoreductase_%28NQO1%29_with_inhibitor_dicoumarol
NADH quinone oxidoreductase (NQO1) with inhibitor dicoumarol - Revision history
2026-09-11T12:17:55Z
Revision history for this page on the wiki
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https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=2577369&oldid=prev
Jaime Prilusky at 04:38, 29 February 2016
2016-02-29T04:38:35Z
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Jaime Prilusky
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=2577368&oldid=prev
Jaime Prilusky at 04:37, 29 February 2016
2016-02-29T04:37:53Z
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Jaime Prilusky
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=2526953&oldid=prev
Michal Harel at 09:00, 2 February 2016
2016-02-02T09:00:34Z
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== The crystal structure of NADH quinone oxidoreductase (NQO1) in complex with its potent inhibitor dicoumarol ==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== The crystal structure of NADH quinone oxidoreductase (NQO1) in complex with its potent inhibitor dicoumarol ==</div></td></tr>
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Michal Harel
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=1878873&oldid=prev
Alexander Berchansky at 14:13, 23 December 2013
2013-12-23T14:13:29Z
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== The crystal structure of NADH quinone oxidoreductase (NQO1) in complex with its potent inhibitor dicoumarol ==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== The crystal structure of NADH quinone oxidoreductase (NQO1) in complex with its potent inhibitor dicoumarol ==</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[Image:NQO_Dic copy.jpg|border|<del style="font-weight: bold; text-decoration: none;">center</del>|300px]]</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[Image:NQO_Dic copy.jpg|border|<ins style="font-weight: bold; text-decoration: none;">left</ins>|300px]]</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">{{Clear}}</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[http://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H quinone oxidoreductase 1] (NQO1, [http://www.expasy.org/cgi-bin/nicezyme.pl?1.6.5.2 EC 1.6.5.2]) is a ubiquitous [http://medical-dictionary.thefreedictionary.com/flavoenzyme flavoenzyme] that [http://en.wikipedia.org/wiki/Catalysis catalyzes] two electron reduction of [http://en.wikipedia.org/wiki/Quinone quinones] to [http://en.wikipedia.org/wiki/Hydroquinone hydroquinones] utilizing [[NAD(P)H]] as an [http://en.wikipedia.org/wiki/Electron_donor electron donor]. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[http://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H quinone oxidoreductase 1] (NQO1, [http://www.expasy.org/cgi-bin/nicezyme.pl?1.6.5.2 EC 1.6.5.2]) is a ubiquitous [http://medical-dictionary.thefreedictionary.com/flavoenzyme flavoenzyme] that [http://en.wikipedia.org/wiki/Catalysis catalyzes] two electron reduction of [http://en.wikipedia.org/wiki/Quinone quinones] to [http://en.wikipedia.org/wiki/Hydroquinone hydroquinones] utilizing [[NAD(P)H]] as an [http://en.wikipedia.org/wiki/Electron_donor electron donor]. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>NQO1 is a homo-dimer that functions via a “ping pong” mechanism. NAD(P)H binds to NQO1, reduces the [http://en.wikipedia.org/wiki/FAD FAD] co-factor and is then released, allowing the quinone substrate to bind the enzyme and to be reduced. The NAD(P)H and the quinone binding sites of NQO1 have a significant overlap, thus providing a molecular basis for this “ping pong” mechanism. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>NQO1 is a homo-dimer that functions via a “ping pong” mechanism. NAD(P)H binds to NQO1, reduces the [http://en.wikipedia.org/wiki/FAD FAD] co-factor and is then released, allowing the quinone substrate to bind the enzyme and to be reduced. The NAD(P)H and the quinone binding sites of NQO1 have a significant overlap, thus providing a molecular basis for this “ping pong” mechanism. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Certain [http://en.wikipedia.org/wiki/Coumarin coumarins], [http://en.wikipedia.org/wiki/Flavones flavones] and the reactive dye cibacron blue are [http://en.wikipedia.org/wiki/Competitive_inhibition competitive inhibitors] of NQO1 activity, which compete with NAD(P)H for binding to NQO1. [[Dicoumarol]] (3-3’–methylene-bis (4-hydroxycoumarin)),[[Image:Figure3 copy.jpg|border|center|300px]] is the most potent competitive inhibitor of NQO1. Dicoumarol competes with NAD(P)H for binding to NQO1 and prevents the [http://en.wikipedia.org/wiki/Electron_transfer electron transfer] to FAD.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Certain [http://en.wikipedia.org/wiki/Coumarin coumarins], [http://en.wikipedia.org/wiki/Flavones flavones] and the reactive dye cibacron blue are [http://en.wikipedia.org/wiki/Competitive_inhibition competitive inhibitors] of NQO1 activity, which compete with NAD(P)H for binding to NQO1. [[Dicoumarol]] (3-3’–methylene-bis (4-hydroxycoumarin)),[[Image:Figure3 copy.jpg|border|center|300px]] is the most potent competitive inhibitor of NQO1. Dicoumarol competes with NAD(P)H for binding to NQO1 and prevents the [http://en.wikipedia.org/wiki/Electron_transfer electron transfer] to FAD.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>In addition to its role in the detoxification of quinones, NQO1 is also a 20S proteasome-associated protein that plays an important role in the stability of the [http://en.wikipedia.org/wiki/Tumor_suppressor_gene tumor suppressor] p53 and several other short-lived proteins including [[p73α]] and ornithine decarboxylase (ODC, ''i.e.'' [[7odc]]). NQO1 binds and stabilizes [[p53]], protecting p53 from [http://en.wikipedia.org/wiki/Proteasome#Ubiquitin-independent_degradation ubiquitin-independent 20S proteasomal degradation]. Dicoumarol and several other inhibitors of NQO1 activity, which compete with NADH for binding to NQO1, disrupt the binding of NQO1 to p53 and induce ubiquitin-independent p53 degradation.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>In addition to its role in the detoxification of quinones, NQO1 is also a 20S proteasome-associated protein that plays an important role in the stability of the [http://en.wikipedia.org/wiki/Tumor_suppressor_gene tumor suppressor] p53 and several other short-lived proteins including [[p73α]] and ornithine decarboxylase (ODC, ''i.e.'' [[7odc]]). NQO1 binds and stabilizes [[p53]], protecting p53 from [http://en.wikipedia.org/wiki/Proteasome#Ubiquitin-independent_degradation ubiquitin-independent 20S proteasomal degradation]. Dicoumarol and several other inhibitors of NQO1 activity, which compete with NADH for binding to NQO1, disrupt the binding of NQO1 to p53 and induce ubiquitin-independent p53 degradation.</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">{{Clear}}</del></div></td><td colspan="2" class="diff-side-added"></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"><StructureSection load='2f1o.pdb' size='500' frame='true' align='right' scene='2f1o/Com_view/2' caption='NADPH dehydrogenase complex with FAD and dicoumarol [[2f1o]]'></del></div></td><td colspan="2" class="diff-side-added"></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>. NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>. NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances. </div></td></tr>
</table>
Alexander Berchansky
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=1400448&oldid=prev
Alexander Berchansky at 08:21, 3 June 2012
2012-06-03T08:21:49Z
<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:21, 3 June 2012</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>==<del style="font-weight: bold; text-decoration: none;">Reference</del>==</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>==<ins style="font-weight: bold; text-decoration: none;">References</ins>==</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol., Asher G, Dym O, Tsvetkov P, Adler J, Shaul Y, Biochemistry. 2006 May 23;45(20)</del>:<del style="font-weight: bold; text-decoration: none;">6372-8. </del>PMID:<del style="font-weight: bold; text-decoration: none;">[http:</del>//<del style="font-weight: bold; text-decoration: none;">www.ncbi.nlm.nih.gov/pubmed/16700548 16700548]</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"><ref group="xtra">PMID</ins>:<ins style="font-weight: bold; text-decoration: none;">10706635</ref> <ref group="xtra"></ins>PMID:<ins style="font-weight: bold; text-decoration: none;">16700548<</ins>/<ins style="font-weight: bold; text-decoration: none;">ref> <references group="xtra"</ins>/<ins style="font-weight: bold; text-decoration: none;">></ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Category: Homo sapiens]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Category: Homo sapiens]]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Category: Single protein]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[Category: Single protein]]</div></td></tr>
</table>
Alexander Berchansky
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=1346479&oldid=prev
Michal Harel at 09:54, 31 January 2012
2012-01-31T09:54:43Z
<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:54, 31 January 2012</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The quinone ES936 causes irreversible inhibition of the NQO1. <scene name='2f1o/Align2/5'>Alignment</scene> of the hNQO1 dimer in complex with <font color='red'><b>ES936 (red)</b></font> ([[1kbq]]) with the hNQO1−dicoumarol complex ([[2f1o]]) yields 0.45Å RMSD for the 546 Cα atoms. The ES936 causes structural change only in the position of Phe 232. The movement of this residue is smaller than that caused by dicoumarol. The <scene name='2f1o/Align2/6'>distance</scene> between Tyr 128 and Phe 232 in the hNQO1−ES936 complex is only ~7 Å, while in the hNQO1−dicoumarol complex it is ~12 Å.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The quinone ES936 causes irreversible inhibition of the NQO1. <scene name='2f1o/Align2/5'>Alignment</scene> of the hNQO1 dimer in complex with <font color='red'><b>ES936 (red)</b></font> ([[1kbq]]) with the hNQO1−dicoumarol complex ([[2f1o]]) yields 0.45Å RMSD for the 546 Cα atoms. The ES936 causes structural change only in the position of Phe 232. The movement of this residue is smaller than that caused by dicoumarol. The <scene name='2f1o/Align2/6'>distance</scene> between Tyr 128 and Phe 232 in the hNQO1−ES936 complex is only ~7 Å, while in the hNQO1−dicoumarol complex it is ~12 Å.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div></StructureSection></div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div></StructureSection></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">==3D structures of NQ01==</ins></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">[[Quinone reductase]]</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
</table>
Michal Harel
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=1280891&oldid=prev
Alexander Berchansky at 09:13, 4 August 2011
2011-08-04T09:13:06Z
<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:13, 4 August 2011</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l5">Line 5:</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>NQO1 is a homo-dimer that functions via a “ping pong” mechanism. NAD(P)H binds to NQO1, reduces the [http://en.wikipedia.org/wiki/FAD FAD] co-factor and is then released, allowing the quinone substrate to bind the enzyme and to be reduced. The NAD(P)H and the quinone binding sites of NQO1 have a significant overlap, thus providing a molecular basis for this “ping pong” mechanism. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>NQO1 is a homo-dimer that functions via a “ping pong” mechanism. NAD(P)H binds to NQO1, reduces the [http://en.wikipedia.org/wiki/FAD FAD] co-factor and is then released, allowing the quinone substrate to bind the enzyme and to be reduced. The NAD(P)H and the quinone binding sites of NQO1 have a significant overlap, thus providing a molecular basis for this “ping pong” mechanism. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Certain [http://en.wikipedia.org/wiki/Coumarin coumarins], [http://en.wikipedia.org/wiki/Flavones flavones] and the reactive dye cibacron blue are [http://en.wikipedia.org/wiki/Competitive_inhibition competitive inhibitors] of NQO1 activity, which compete with NAD(P)H for binding to NQO1. [[Dicoumarol]] (3-3’–methylene-bis (4-hydroxycoumarin)),[[Image:Figure3 copy.jpg|border|center|300px]] is the most potent competitive inhibitor of NQO1. Dicoumarol competes with NAD(P)H for binding to NQO1 and prevents the [http://en.wikipedia.org/wiki/Electron_transfer electron transfer] to FAD.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Certain [http://en.wikipedia.org/wiki/Coumarin coumarins], [http://en.wikipedia.org/wiki/Flavones flavones] and the reactive dye cibacron blue are [http://en.wikipedia.org/wiki/Competitive_inhibition competitive inhibitors] of NQO1 activity, which compete with NAD(P)H for binding to NQO1. [[Dicoumarol]] (3-3’–methylene-bis (4-hydroxycoumarin)),[[Image:Figure3 copy.jpg|border|center|300px]] is the most potent competitive inhibitor of NQO1. Dicoumarol competes with NAD(P)H for binding to NQO1 and prevents the [http://en.wikipedia.org/wiki/Electron_transfer electron transfer] to FAD.</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>In addition to its role in the detoxification of quinones, NQO1 is also a 20S proteasome-associated protein that plays an important role in the stability of the [http://en.wikipedia.org/wiki/Tumor_suppressor_gene tumor suppressor] p53 and several other short-lived proteins including [[p73α]] and ornithine decarboxylase (<del style="font-weight: bold; text-decoration: none;">[[</del>ODC<del style="font-weight: bold; text-decoration: none;">]]</del>, ''i.e.'' [[7odc]]). NQO1 binds and stabilizes [[p53]], protecting p53 from [http://en.wikipedia.org/wiki/Proteasome#Ubiquitin-independent_degradation ubiquitin-independent 20S proteasomal degradation]. Dicoumarol and several other inhibitors of NQO1 activity, which compete with NADH for binding to NQO1, disrupt the binding of NQO1 to p53 and induce ubiquitin-independent p53 degradation.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>In addition to its role in the detoxification of quinones, NQO1 is also a 20S proteasome-associated protein that plays an important role in the stability of the [http://en.wikipedia.org/wiki/Tumor_suppressor_gene tumor suppressor] p53 and several other short-lived proteins including [[p73α]] and ornithine decarboxylase (ODC, ''i.e.'' [[7odc]]). NQO1 binds and stabilizes [[p53]], protecting p53 from [http://en.wikipedia.org/wiki/Proteasome#Ubiquitin-independent_degradation ubiquitin-independent 20S proteasomal degradation]. Dicoumarol and several other inhibitors of NQO1 activity, which compete with NADH for binding to NQO1, disrupt the binding of NQO1 to p53 and induce ubiquitin-independent p53 degradation.</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Clear}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Clear}}</div></td></tr>
</table>
Alexander Berchansky
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=1280863&oldid=prev
Michal Harel at 06:42, 4 August 2011
2011-08-04T06:42:29Z
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Clear}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Clear}}</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><StructureSection load='2f1o.pdb' size='500' frame='true' align='right' scene='2f1o/Com_view/2' caption=NADPH dehydrogenase complex with FAD and dicoumarol [[2f1o]]></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><StructureSection load='2f1o.pdb' size='500' frame='true' align='right' scene='2f1o/Com_view/2' caption=<ins style="font-weight: bold; text-decoration: none;">'</ins>NADPH dehydrogenase complex with FAD and dicoumarol [[2f1o]]<ins style="font-weight: bold; text-decoration: none;">'</ins>></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>. NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>. NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances. </div></td></tr>
</table>
Michal Harel
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=1280862&oldid=prev
Michal Harel at 06:41, 4 August 2011
2011-08-04T06:41:53Z
<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
<col class="diff-marker" />
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<col class="diff-content" />
<tr class="diff-title" lang="en">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 06:41, 4 August 2011</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l8">Line 8:</td>
<td colspan="2" class="diff-lineno">Line 8:</td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Clear}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Clear}}</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><StructureSection load='2f1o.pdb' size='500' frame='true' align='right' scene='2f1o/Com_view/2' caption=<del style="font-weight: bold; text-decoration: none;">nqo1</del>></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><StructureSection load='2f1o.pdb' size='500' frame='true' align='right' scene='2f1o/Com_view/2' caption=<ins style="font-weight: bold; text-decoration: none;">NADPH dehydrogenase complex with FAD and dicoumarol [[2f1o]]</ins>></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>. NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>. NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances. </div></td></tr>
</table>
Michal Harel
https://proteopedia.org/index.php?title=NADH_quinone_oxidoreductase_(NQO1)_with_inhibitor_dicoumarol&diff=1280861&oldid=prev
Michal Harel at 06:37, 4 August 2011
2011-08-04T06:37:54Z
<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 06:37, 4 August 2011</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l8">Line 8:</td>
<td colspan="2" class="diff-lineno">Line 8:</td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Clear}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Clear}}</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><StructureSection load='2f1o.pdb' size='500' frame='true' align='right' scene='2f1o/Com_view/2' ></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><StructureSection load='2f1o.pdb' size='500' frame='true' align='right' scene='2f1o/Com_view/2' <ins style="font-weight: bold; text-decoration: none;"> caption=nqo1</ins>></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>. NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>. NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances. </div></td></tr>
</table>
Michal Harel