3qmu - Revision history

OCA: Redirecting to 6dhq

OCA — Wed, 25 Jul 2018 07:05:14 GMT

Redirecting to 6dhq

←Older revision		Revision as of 07:05, 25 July 2018
Line 1:		Line 1:
-		+	#REDIRECT [[6dhq]] This PDB entry is obsolete and replaced by 6dhq
-	~~==Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)==~~	+
-	~~<StructureSection load='3qmu' size='340' side='right' caption='~~[[~~3qmu]], [[Resolution\|resolution]] 3.62Å' scene=''>~~	+
-	~~== Structural highlights ==~~	+
-	~~<table><tr><td colspan='2'>[[3qmu~~]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QMU FirstGlance]. <br>	+
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=XEG:(2R,3S)-2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-3,4-DIHYDRO-2H-CHROMEN-3-YL+3,4,5-TRIHYDROXYBENZOATE'>XEG</scene></td></tr>	+
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mw9\|3mw9]], [[1nqt\|1nqt]], [[1nr7\|1nr7]], [[1hwy\|1hwy]], [[1hwz\|1hwz]], [[3ete\|3ete]]</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmu OCA], [http://pdbe.org/3qmu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qmu RCSB], [http://www.ebi.ac.uk/pdbsum/3qmu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmu ProSAT]</span></td></tr>	+
-	~~</table>~~	+
-	~~== Function ==~~	+
-	~~[[http://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN]] May be involved in learning~~ and ~~memory reactions~~ by ~~increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>~~	+
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Glutamate dehydrogenase (GDH) catalyzes the oxidative deamination of L-glutamate and, in animals, is extensively regulated by a number of metabolites. Gain of function mutations in GDH that abrogate GTP inhibition causes the hyperinsulinism/hyperammonemia syndrome (HHS), resulting in increased pancreatic beta-cells responsiveness to leucine and susceptibility to hypoglycemia following high protein meals. We have previously shown that two of the polyphenols from green tea (EGCG and ECG) inhibit GDH in-vitro and that EGCG blocks GDH-mediated insulin secretion in wild type rat islets. Using structural and site-directed mutagenesis studies, we demonstrate that ECG binds to the same site as the allosteric regulator, ADP. Perifusion assays using pancreatic islets from transgenic mice expressing a human HHS form of GDH demonstrate that the hyper-response to glutamine caused by dysregulated GDH is blocked by the addition of EGCG. As observed in HHS patients, these transgenic mice are hypersensitive to amino acid feeding and this is abrogated by oral administration of EGCG prior to challenge. Finally, the low basal blood glucose level in the HHS mouse model is improved upon chronic administration of EGCG. These results suggest that this common natural product, or some derivative thereof, may prove useful in controlling this genetic disorder. Of broader clinical implication is that other groups have shown restriction of glutamine catabolism via these GDH inhibitors can be useful in treating various tumors. This HHS transgenic mouse model offers a highly useful means to test these agents in-vivo.	+
-		+
-	GREEN TEA POLYPHENOLS CONTROL DYSREGULATED GLUTAMATE DEHYDROGENASE IN TRANSGENIC MICE BY HIJACKING THE ADP ACTIVATION SITE.,Li C, Li M, Chen P, Narayan S, Matschinsky FM, Bennett MJ, Stanley C, Smith TJ J Biol Chem. 2011 Aug 3. PMID:21813650<ref>PMID:21813650</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3qmu" style="background-color:#fffaf0;"></div>~~	+
-		+
-	~~==See Also==~~	+
-	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]	+
-	~~== References ==~~	+
-	~~<references/>~~	+
-	~~__TOC__~~	+
-	~~</StructureSection>~~	+
-	~~[[Category: Bos taurus]]~~	+
-	~~[[Category: Li, C]]~~	+
-	~~[[Category: Li, M]]~~	+
-	~~[[Category: Smith, T J]]~~	+
-	~~[[Category: Stanley, C]]~~	+
-	~~[[Category: Dehydrogenase]]~~	+
-	~~[[Category: Mitochondria]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Rossmann fold]]~~	+

OCA at 22:59, 4 August 2016

OCA — Thu, 04 Aug 2016 22:59:27 GMT

←Older revision		Revision as of 22:59, 4 August 2016
Line 1:		Line 1:
		+
	==Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)==		==Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)==
	<StructureSection load='3qmu' size='340' side='right' caption='[[3qmu]], [[Resolution\|resolution]] 3.62Å' scene=''>		<StructureSection load='3qmu' size='340' side='right' caption='[[3qmu]], [[Resolution\|resolution]] 3.62Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mw9\|3mw9]], [[1nqt\|1nqt]], [[1nr7\|1nr7]], [[1hwy\|1hwy]], [[1hwz\|1hwz]], [[3ete\|3ete]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mw9\|3mw9]], [[1nqt\|1nqt]], [[1nr7\|1nr7]], [[1hwy\|1hwy]], [[1hwz\|1hwz]], [[3ete\|3ete]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qmu RCSB], [http://www.ebi.ac.uk/pdbsum/3qmu PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmu OCA], [http://pdbe.org/3qmu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qmu RCSB], [http://www.ebi.ac.uk/pdbsum/3qmu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3qmu" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 20:27, 24 December 2014

OCA — Wed, 24 Dec 2014 20:27:37 GMT

←Older revision		Revision as of 20:27, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3qmu]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QMU FirstGlance]. <br>		<table><tr><td colspan='2'>[[3qmu]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QMU FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=XEG:(2R,3S)-2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-3,4-DIHYDRO-2H-CHROMEN-3-YL+3,4,5-TRIHYDROXYBENZOATE'>XEG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=XEG:(2R,3S)-2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-3,4-DIHYDRO-2H-CHROMEN-3-YL+3,4,5-TRIHYDROXYBENZOATE'>XEG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mw9\|3mw9]], [[1nqt\|1nqt]], [[1nr7\|1nr7]], [[1hwy\|1hwy]], [[1hwz\|1hwz]], [[3ete\|3ete]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mw9\|3mw9]], [[1nqt\|1nqt]], [[1nr7\|1nr7]], [[1hwy\|1hwy]], [[1hwz\|1hwz]], [[3ete\|3ete]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qmu RCSB], [http://www.ebi.ac.uk/pdbsum/3qmu PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qmu RCSB], [http://www.ebi.ac.uk/pdbsum/3qmu PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN]] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 16:
	GREEN TEA POLYPHENOLS CONTROL DYSREGULATED GLUTAMATE DEHYDROGENASE IN TRANSGENIC MICE BY HIJACKING THE ADP ACTIVATION SITE.,Li C, Li M, Chen P, Narayan S, Matschinsky FM, Bennett MJ, Stanley C, Smith TJ J Biol Chem. 2011 Aug 3. PMID:21813650<ref>PMID:21813650</ref>		GREEN TEA POLYPHENOLS CONTROL DYSREGULATED GLUTAMATE DEHYDROGENASE IN TRANSGENIC MICE BY HIJACKING THE ADP ACTIVATION SITE.,Li C, Li M, Chen P, Narayan S, Matschinsky FM, Bennett MJ, Stanley C, Smith TJ J Biol Chem. 2011 Aug 3. PMID:21813650<ref>PMID:21813650</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>

Line 24:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Li, C.]]	+	[[Category: Li, C]]
-	[[Category: Li, M.]]	+	[[Category: Li, M]]
-	[[Category: Smith, T J.]]	+	[[Category: Smith, T J]]
-	[[Category: Stanley, C.]]	+	[[Category: Stanley, C]]
	[[Category: Dehydrogenase]]		[[Category: Dehydrogenase]]
	[[Category: Mitochondria]]		[[Category: Mitochondria]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Rossmann fold]]		[[Category: Rossmann fold]]

OCA at 05:29, 4 June 2014

OCA — Wed, 04 Jun 2014 05:29:02 GMT

←Older revision		Revision as of 05:29, 4 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3qmu.~~png~~\|~~left~~\|~~200px~~]]	+	==Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)==
		+	<StructureSection load='3qmu' size='340' side='right' caption='[[3qmu]], [[Resolution\|resolution]] 3.62Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3qmu]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QMU FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=XEG:(2R,3S)-2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-3,4-DIHYDRO-2H-CHROMEN-3-YL+3,4,5-TRIHYDROXYBENZOATE'>XEG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mw9\|3mw9]], [[1nqt\|1nqt]], [[1nr7\|1nr7]], [[1hwy\|1hwy]], [[1hwz\|1hwz]], [[3ete\|3ete]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qmu RCSB], [http://www.ebi.ac.uk/pdbsum/3qmu PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glutamate dehydrogenase (GDH) catalyzes the oxidative deamination of L-glutamate and, in animals, is extensively regulated by a number of metabolites. Gain of function mutations in GDH that abrogate GTP inhibition causes the hyperinsulinism/hyperammonemia syndrome (HHS), resulting in increased pancreatic beta-cells responsiveness to leucine and susceptibility to hypoglycemia following high protein meals. We have previously shown that two of the polyphenols from green tea (EGCG and ECG) inhibit GDH in-vitro and that EGCG blocks GDH-mediated insulin secretion in wild type rat islets. Using structural and site-directed mutagenesis studies, we demonstrate that ECG binds to the same site as the allosteric regulator, ADP. Perifusion assays using pancreatic islets from transgenic mice expressing a human HHS form of GDH demonstrate that the hyper-response to glutamine caused by dysregulated GDH is blocked by the addition of EGCG. As observed in HHS patients, these transgenic mice are hypersensitive to amino acid feeding and this is abrogated by oral administration of EGCG prior to challenge. Finally, the low basal blood glucose level in the HHS mouse model is improved upon chronic administration of EGCG. These results suggest that this common natural product, or some derivative thereof, may prove useful in controlling this genetic disorder. Of broader clinical implication is that other groups have shown restriction of glutamine catabolism via these GDH inhibitors can be useful in treating various tumors. This HHS transgenic mouse model offers a highly useful means to test these agents in-vivo.

-	~~<!--~~	+	GREEN TEA POLYPHENOLS CONTROL DYSREGULATED GLUTAMATE DEHYDROGENASE IN TRANSGENIC MICE BY HIJACKING THE ADP ACTIVATION SITE.,Li C, Li M, Chen P, Narayan S, Matschinsky FM, Bennett MJ, Stanley C, Smith TJ J Biol Chem. 2011 Aug 3. PMID:21813650<ref>PMID:21813650</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3qmu"~~, ~~creates the "Structure Box" on the page.~~	+
-	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded)~~,	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_3qmu\| PDB=3qmu \| SCENE= }}~~	+

-	~~===Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	~~<!--~~	+	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21813650}}, adds the Publication Abstract to the page~~	+	== References ==
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 21813650 is the PubMed ID number.~~	+	<references/>
-	~~-->~~	+	__TOC__
-	~~{{ABSTRACT_PUBMED_21813650}}~~	+	</StructureSection>
-		+
-	==~~About this Structure~~==	+
-	[[~~3qmu~~]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMU OCA].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:021813650<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Li, C.]]		[[Category: Li, C.]]

OCA at 06:14, 17 August 2011

OCA — Wed, 17 Aug 2011 06:14:35 GMT

←Older revision		Revision as of 06:14, 17 August 2011
Line 1:		Line 1:
-	[[Image:3qmu.~~jpg~~\|left\|200px]]	+	[[Image:3qmu.png\|left\|200px]]

	<!--		<!--
Line 11:		Line 11:
	===Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)===		===Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21813650}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21813650 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21813650}}

	==About this Structure==		==About this Structure==
	[[3qmu]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMU OCA].		[[3qmu]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMU OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021813650</ref><references group="xtra"/>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Li, C.]]		[[Category: Li, C.]]

OCA at 08:58, 3 August 2011

OCA — Wed, 03 Aug 2011 08:58:48 GMT

←Older revision		Revision as of 08:58, 3 August 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3qmu.jpg\|left\|200px]]

-	The ~~entry 3qmu~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3qmu", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3qmu\| PDB=3qmu \| SCENE= }}

-	~~Authors: Li, C., Li, M., Stanley, C., Smith, T.J.~~	+	===Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)===

-	~~Description: Bovine glutamate dehydrogenase complexed~~ with ~~epicatechin~~-~~3-gallate (ECG)~~	+
		+	==About this Structure==
		+	[[3qmu]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMU OCA].
		+	[[Category: Bos taurus]]
		+	[[Category: Li, C.]]
		+	[[Category: Li, M.]]
		+	[[Category: Smith, T J.]]
		+	[[Category: Stanley, C.]]
		+	[[Category: Dehydrogenase]]
		+	[[Category: Mitochondria]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Rossmann fold]]

OCA: Protected "3qmu" [edit=sysop:move=sysop]

OCA — Wed, 16 Feb 2011 05:22:30 GMT

Protected "3qmu" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:22, 16 February 2011

OCA: New page: '''Unreleased structure''' The entry 3qmu is ON HOLD until Paper Publication Authors: Li, C., Li, M., Stanley, C., Smith, T.J. Description: Bovine glutamate dehydrogenase complexed wit...

OCA — Wed, 16 Feb 2011 05:22:29 GMT

New page: '''Unreleased structure''' The entry 3qmu is ON HOLD until Paper Publication Authors: Li, C., Li, M., Stanley, C., Smith, T.J. Description: Bovine glutamate dehydrogenase complexed wit...

New page

'''Unreleased structure'''

The entry 3qmu is ON HOLD until Paper Publication

Authors: Li, C., Li, M., Stanley, C., Smith, T.J.

Description: Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)