4g1n - Revision history

OCA at 11:24, 1 March 2024

OCA — Fri, 01 Mar 2024 11:24:59 GMT

←Older revision		Revision as of 11:24, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g1n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G1N FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g1n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G1N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NZT:N-(4-{[4-(PYRAZIN-2-YL)PIPERAZIN-1-YL]CARBONYL}PHENYL)QUINOLINE-8-SULFONAMIDE'>NZT</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NZT:N-(4-{[4-(PYRAZIN-2-YL)PIPERAZIN-1-YL]CARBONYL}PHENYL)QUINOLINE-8-SULFONAMIDE'>NZT</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [https://pdbe.org/4g1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [https://www.ebi.ac.uk/pdbsum/4g1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g1n ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [https://pdbe.org/4g1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [https://www.ebi.ac.uk/pdbsum/4g1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g1n ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/KPYM_HUMAN KPYM_HUMAN] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.<ref>PMID:17308100</ref> <ref>PMID:18191611</ref> <ref>PMID:21620138</ref>		[https://www.uniprot.org/uniprot/KPYM_HUMAN KPYM_HUMAN] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.<ref>PMID:17308100</ref> <ref>PMID:18191611</ref> <ref>PMID:21620138</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Proliferating tumor cells use aerobic glycolysis to support their high metabolic demands. Paradoxically, increased glycolysis is often accompanied by expression of the lower activity PKM2 isoform, effectively constraining lower glycolysis. Here, we report the discovery of PKM2 activators with a unique allosteric binding mode. Characterization of how these compounds impact cancer cells revealed an unanticipated link between glucose and amino acid metabolism. PKM2 activation resulted in a metabolic rewiring of cancer cells manifested by a profound dependency on the nonessential amino acid serine for continued cell proliferation. Induction of serine auxotrophy by PKM2 activation was accompanied by reduced carbon flow into the serine biosynthetic pathway and increased expression of high affinity serine transporters. These data support the hypothesis that PKM2 expression confers metabolic flexibility to cancer cells that allows adaptation to nutrient stress.
-
-	Small Molecule Activation of PKM2 in Cancer Cells Induces Serine Auxotrophy.,Kung C, Hixon J, Choe S, Marks K, Gross S, Murphy E, Delabarre B, Cianchetta G, Sethumadhavan S, Wang X, Yan S, Gao Y, Fang C, Wei W, Jiang F, Wang S, Qian K, Saunders J, Driggers E, Woo HK, Kunii K, Murray S, Yang H, Yen K, Liu W, Cantley LC, Vander Heiden MG, Su SM, Jin S, Salituro FG, Dang L Chem Biol. 2012 Sep 21;19(9):1187-98. doi: 10.1016/j.chembiol.2012.07.021. PMID:22999886<ref>PMID:22999886</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4g1n" style="background-color:#fffaf0;"></div>

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

OCA at 20:20, 19 October 2022

OCA — Wed, 19 Oct 2022 20:20:02 GMT

←Older revision		Revision as of 20:20, 19 October 2022
Line 1:		Line 1:

	==PKM2 in complex with an activator==		==PKM2 in complex with an activator==
-	<StructureSection load='4g1n' size='340' side='right' caption='[[4g1n]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='4g1n' size='340' side='right'caption='[[4g1n]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4g1n]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4G1N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4g1n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G1N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NZT:N-(4-{[4-(PYRAZIN-2-YL)PIPERAZIN-1-YL]CARBONYL}PHENYL)QUINOLINE-8-SULFONAMIDE'>NZT</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NZT:N-(4-{[4-(PYRAZIN-2-YL)PIPERAZIN-1-YL]CARBONYL}PHENYL)QUINOLINE-8-SULFONAMIDE'>NZT</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PKM2, OIP3, PK2, PK3, PKM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [https://pdbe.org/4g1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [https://www.ebi.ac.uk/pdbsum/4g1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g1n ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </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=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [~~http~~://pdbe.org/4g1n PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4g1n PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4g1n ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KPYM_HUMAN KPYM_HUMAN]] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.<ref>PMID:17308100</ref> <ref>PMID:18191611</ref> <ref>PMID:21620138</ref>	+	[https://www.uniprot.org/uniprot/KPYM_HUMAN KPYM_HUMAN] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.<ref>PMID:17308100</ref> <ref>PMID:18191611</ref> <ref>PMID:21620138</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Pyruvate ~~Kinase~~\|Pyruvate ~~Kinase~~]]	+	*[[Pyruvate kinase 3D structures\|Pyruvate kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Pyruvate kinase~~]]	+	[[Category: Large Structures]]
-	[[Category: Dang, L]]	+	[[Category: Dang L]]
-	[[Category: DeLaBarre, B]]	+	[[Category: DeLaBarre B]]
-	[[Category: Hixon, J]]	+	[[Category: Hixon J]]
-	[[Category: Kung, C]]	+	[[Category: Kung C]]
-	[[Category: Qian~~, K C]]~~	+	[[Category: Qian KC]]
-	~~[[Category: Activator]]~~	+
-	~~[[Category: Aerobic glycolysis]]~~	+
-	~~[[Category: Cancer metabolism]]~~	+
-	~~[[Category: Phosphorylation of pyruvate]]~~	+
-	~~[[Category: Transferase-activator complex~~]]	+

OCA at 11:19, 5 August 2016

OCA — Fri, 05 Aug 2016 11:19:47 GMT

←Older revision		Revision as of 11:19, 5 August 2016
Line 1:		Line 1:
		+
	==PKM2 in complex with an activator==		==PKM2 in complex with an activator==
	<StructureSection load='4g1n' size='340' side='right' caption='[[4g1n]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4g1n' size='340' side='right' caption='[[4g1n]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PKM2, OIP3, PK2, PK3, PKM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PKM2, OIP3, PK2, PK3, PKM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </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=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [http://www.ebi.ac.uk/pdbsum/4g1n 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=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [http://pdbe.org/4g1n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [http://www.ebi.ac.uk/pdbsum/4g1n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g1n 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 4g1n" style="background-color:#fffaf0;"></div>

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

OCA at 01:58, 25 December 2014

OCA — Thu, 25 Dec 2014 01:58:04 GMT

←Older revision		Revision as of 01:58, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g1n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G1N FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g1n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G1N FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NZT:N-(4-{[4-(PYRAZIN-2-YL)PIPERAZIN-1-YL]CARBONYL}PHENYL)QUINOLINE-8-SULFONAMIDE'>NZT</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NZT:N-(4-{[4-(PYRAZIN-2-YL)PIPERAZIN-1-YL]CARBONYL}PHENYL)QUINOLINE-8-SULFONAMIDE'>NZT</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PKM2, OIP3, PK2, PK3, PKM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PKM2, OIP3, PK2, PK3, PKM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </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=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [http://www.ebi.ac.uk/pdbsum/4g1n 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=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [http://www.ebi.ac.uk/pdbsum/4g1n PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KPYM_HUMAN KPYM_HUMAN]] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.<ref>PMID:17308100</ref> <ref>PMID:18191611</ref> <ref>PMID:21620138</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 27:
	[[Category: Human]]		[[Category: Human]]
	[[Category: Pyruvate kinase]]		[[Category: Pyruvate kinase]]
-	[[Category: Dang, L.]]	+	[[Category: Dang, L]]
-	[[Category: DeLaBarre, B.]]	+	[[Category: DeLaBarre, B]]
-	[[Category: Hixon, J.]]	+	[[Category: Hixon, J]]
-	[[Category: Kung, C.]]	+	[[Category: Kung, C]]
-	[[Category: Qian, K C.]]	+	[[Category: Qian, K C]]
	[[Category: Activator]]		[[Category: Activator]]
	[[Category: Aerobic glycolysis]]		[[Category: Aerobic glycolysis]]
	[[Category: Cancer metabolism]]		[[Category: Cancer metabolism]]
	[[Category: Phosphorylation of pyruvate]]		[[Category: Phosphorylation of pyruvate]]
-	[[Category: Pyruvate kinase]]
	[[Category: Transferase-activator complex]]		[[Category: Transferase-activator complex]]

OCA at 10:44, 16 July 2014

OCA — Wed, 16 Jul 2014 10:44:02 GMT

←Older revision		Revision as of 10:44, 16 July 2014
Line 1:		Line 1:
-	[[~~Image:~~4g1n.~~jpg~~\|~~left~~\|~~200px~~]]	+	==PKM2 in complex with an activator==
		+	<StructureSection load='4g1n' size='340' side='right' caption='[[4g1n]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4g1n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G1N FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NZT:N-(4-{[4-(PYRAZIN-2-YL)PIPERAZIN-1-YL]CARBONYL}PHENYL)QUINOLINE-8-SULFONAMIDE'>NZT</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PKM2, OIP3, PK2, PK3, PKM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </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=4g1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g1n RCSB], [http://www.ebi.ac.uk/pdbsum/4g1n PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Proliferating tumor cells use aerobic glycolysis to support their high metabolic demands. Paradoxically, increased glycolysis is often accompanied by expression of the lower activity PKM2 isoform, effectively constraining lower glycolysis. Here, we report the discovery of PKM2 activators with a unique allosteric binding mode. Characterization of how these compounds impact cancer cells revealed an unanticipated link between glucose and amino acid metabolism. PKM2 activation resulted in a metabolic rewiring of cancer cells manifested by a profound dependency on the nonessential amino acid serine for continued cell proliferation. Induction of serine auxotrophy by PKM2 activation was accompanied by reduced carbon flow into the serine biosynthetic pathway and increased expression of high affinity serine transporters. These data support the hypothesis that PKM2 expression confers metabolic flexibility to cancer cells that allows adaptation to nutrient stress.

-	~~{{STRUCTURE_4g1n\| PDB=4g1n \| SCENE= }}~~	+	Small Molecule Activation of PKM2 in Cancer Cells Induces Serine Auxotrophy.,Kung C, Hixon J, Choe S, Marks K, Gross S, Murphy E, Delabarre B, Cianchetta G, Sethumadhavan S, Wang X, Yan S, Gao Y, Fang C, Wei W, Jiang F, Wang S, Qian K, Saunders J, Driggers E, Woo HK, Kunii K, Murray S, Yang H, Yen K, Liu W, Cantley LC, Vander Heiden MG, Su SM, Jin S, Salituro FG, Dang L Chem Biol. 2012 Sep 21;19(9):1187-98. doi: 10.1016/j.chembiol.2012.07.021. PMID:22999886<ref>PMID:22999886</ref>

-	~~===PKM2 in complex with an activator===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_22999886}}~~	+	==See Also==
-		+	*[[Pyruvate Kinase\|Pyruvate Kinase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4g1n~~]] ~~is a 4 chain structure. Full crystallographic information is available from [http:~~//~~oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA~~].	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
	[[Category: Pyruvate kinase]]		[[Category: Pyruvate kinase]]
	[[Category: Dang, L.]]		[[Category: Dang, L.]]

OCA at 07:19, 10 October 2012

OCA — Wed, 10 Oct 2012 07:19:39 GMT

←Older revision		Revision as of 07:19, 10 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4g1n.jpg\|left\|200px]]

-	~~The entry~~ 4g1n ~~is ON HOLD~~	+	{{STRUCTURE_4g1n\| PDB=4g1n \| SCENE= }}

-	~~Authors: Kung, C., Hixon, J., Dang, L., DeLaBarre, B., Qian, K.C.~~	+	===PKM2 in complex with an activator===

-	~~Description~~: ~~PKM2 in complex with an~~ activator	+	{{ABSTRACT_PUBMED_22999886}}
		+
		+	==About this Structure==
		+	[[4g1n]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1N OCA].
		+	[[Category: Pyruvate kinase]]
		+	[[Category: Dang, L.]]
		+	[[Category: DeLaBarre, B.]]
		+	[[Category: Hixon, J.]]
		+	[[Category: Kung, C.]]
		+	[[Category: Qian, K C.]]
		+	[[Category: Activator]]
		+	[[Category: Aerobic glycolysis]]
		+	[[Category: Cancer metabolism]]
		+	[[Category: Phosphorylation of pyruvate]]
		+	[[Category: Pyruvate kinase]]
		+	[[Category: Transferase-activator complex]]

OCA: Protected "4g1n" [edit=sysop:move=sysop]

OCA — Wed, 18 Jul 2012 05:08:11 GMT

Protected "4g1n" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:08, 18 July 2012

OCA: New page: '''Unreleased structure''' The entry 4g1n is ON HOLD Authors: Kung, C., Hixon, J., Dang, L., DeLaBarre, B., Qian, K.C. Description: PKM2 in complex with an activator

OCA — Wed, 18 Jul 2012 05:08:10 GMT

New page: '''Unreleased structure''' The entry 4g1n is ON HOLD Authors: Kung, C., Hixon, J., Dang, L., DeLaBarre, B., Qian, K.C. Description: PKM2 in complex with an activator

New page

'''Unreleased structure'''

The entry 4g1n is ON HOLD

Authors: Kung, C., Hixon, J., Dang, L., DeLaBarre, B., Qian, K.C.

Description: PKM2 in complex with an activator