4l4s - Revision history

OCA at 12:17, 1 March 2024

2024-03-01T12:17:11Z

←Older revision		Revision as of 12:17, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4l4s]] is a 2 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=4L4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L4S FirstGlance]. <br>		<table><tr><td colspan='2'>[[4l4s]] is a 2 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=4L4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L4S FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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]] 2.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [https://pdbe.org/4l4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [https://www.ebi.ac.uk/pdbsum/4l4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l4s 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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [https://pdbe.org/4l4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [https://www.ebi.ac.uk/pdbsum/4l4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l4s ProSAT]</span></td></tr>
	</table>		</table>
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	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]		[https://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Lactate dehydrogenase A (LDH-A) is a key enzyme in anaerobic respiration that is predominantly found in skeletal muscle and catalyses the reversible conversion of pyruvate to lactate in the presence of NADH. LDH-A is overexpressed in many tumours and has therefore emerged as an attractive target for anticancer drug discovery. Crystal structures of human LDH-A in the presence of inhibitors have been described, but currently no structures of the apo or binary NADH-bound forms are available for any mammalian LDH-A. Here, the apo structure of human LDH-A was solved at a resolution of 2.1 A in space group P4122. The active-site loop adopts an open conformation and the packing and crystallization conditions suggest that the crystal form is suitable for soaking experiments. The soaking potential was assessed with the cofactor NADH, which yielded a ligand-bound crystal structure in the absence of any inhibitors. The structures show that NADH binding induces small conformational changes in the active-site loop and an adjacent helix. A comparison with other eukaryotic apo LDH structures reveals the conservation of intra-loop interactions. The structures provide novel insight into cofactor binding and provide the foundation for soaking experiments with fragments and inhibitors.
-
-	Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase.,Dempster S, Harper S, Moses JE, Dreveny I Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1484-90. doi:, 10.1107/S1399004714005422. Epub 2014 Apr 30. PMID:24816116<ref>PMID:24816116</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4l4s" style="background-color:#fffaf0;"></div>

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

OCA at 09:32, 7 December 2022

2022-12-07T09:32:33Z

←Older revision		Revision as of 09:32, 7 December 2022
Line 1:		Line 1:

	==Structural characterisation of the NADH binary complex of human lactate dehydrogenase M isozyme==		==Structural characterisation of the NADH binary complex of human lactate dehydrogenase M isozyme==
-	<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='4l4s' size='340' side='right'caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4l4s]] is a 2 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=4L4S OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4L4S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4l4s]] is a 2 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=4L4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L4S FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l4r\|4l4r]]</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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [https://pdbe.org/4l4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [https://www.ebi.ac.uk/pdbsum/4l4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l4s ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LDHA, PIG19 ([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/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [~~http~~://pdbe.org/4l4s PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4l4s PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4l4s ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[~~http~~://omim.org/entry/612933 612933]]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>	+	[https://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[https://omim.org/entry/612933 612933]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4l4s" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4l4s" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Lactate dehydrogenase 3D structures\|Lactate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~L-lactate dehydrogenase~~]]	+	[[Category: Large Structures]]
-	[[Category: Dempster, S]]	+	[[Category: Dempster S]]
-	[[Category: Dreveny, I]]	+	[[Category: Dreveny I]]
-	[[Category: Harper, S]]	+	[[Category: Harper S]]
-	[[Category: Moses~~, J E]]~~	+	[[Category: Moses JE]]
-	~~[[Category: Anaerobic respiration]]~~	+
-	~~[[Category: Glycolysis]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 14:27, 5 August 2016

2016-08-05T14:27:46Z

←Older revision		Revision as of 14:27, 5 August 2016
Line 1:		Line 1:
		+
	==Structural characterisation of the NADH binary complex of human lactate dehydrogenase M isozyme==		==Structural characterisation of the NADH binary complex of human lactate dehydrogenase M isozyme==
	<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LDHA, PIG19 ([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">LDHA, PIG19 ([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/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s 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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://pdbe.org/4l4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l4s ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	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 4l4s" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:14, 25 December 2014

2014-12-25T03:14:49Z

←Older revision		Revision as of 03:14, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4l4s]] is a 2 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=4L4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L4S FirstGlance]. <br>		<table><tr><td colspan='2'>[[4l4s]] is a 2 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=4L4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L4S FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l4r\|4l4r]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l4r\|4l4r]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LDHA, PIG19 ([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">LDHA, PIG19 ([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/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s 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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[http://omim.org/entry/612933 612933]]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>		[[http://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[http://omim.org/entry/612933 612933]]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>
-	== Function ==
-
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 17:
	Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase.,Dempster S, Harper S, Moses JE, Dreveny I Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1484-90. doi:, 10.1107/S1399004714005422. Epub 2014 Apr 30. PMID:24816116<ref>PMID:24816116</ref>		Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase.,Dempster S, Harper S, Moses JE, Dreveny I Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1484-90. doi:, 10.1107/S1399004714005422. Epub 2014 Apr 30. PMID:24816116<ref>PMID:24816116</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>
	== References ==		== References ==
Line 27:		Line 25:
	[[Category: Human]]		[[Category: Human]]
	[[Category: L-lactate dehydrogenase]]		[[Category: L-lactate dehydrogenase]]
-	[[Category: Dempster, S.]]	+	[[Category: Dempster, S]]
-	[[Category: Dreveny, I.]]	+	[[Category: Dreveny, I]]
-	[[Category: Harper, S.]]	+	[[Category: Harper, S]]
-	[[Category: Moses, J E.]]	+	[[Category: Moses, J E]]
	[[Category: Anaerobic respiration]]		[[Category: Anaerobic respiration]]
	[[Category: Glycolysis]]		[[Category: Glycolysis]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 04:33, 4 June 2014

2014-06-04T04:33:37Z

←Older revision		Revision as of 04:33, 4 June 2014
Line 2:		Line 2:
	<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4l4s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L4S OCA]. <br>	+	<table><tr><td colspan='2'>[[4l4s]] is a 2 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=4L4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L4S FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene><br>		</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene><br>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l4r\|4l4r]]</td></tr>		<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l4r\|4l4r]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.~~2 2~~.7.1.2] </span></td></tr>	+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LDHA, PIG19 ([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/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s PDBsum]</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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s PDBsum]</span></td></tr>
	<table>		<table>
Line 12:		Line 13:
	== Function ==		== Function ==

		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Lactate dehydrogenase A (LDH-A) is a key enzyme in anaerobic respiration that is predominantly found in skeletal muscle and catalyses the reversible conversion of pyruvate to lactate in the presence of NADH. LDH-A is overexpressed in many tumours and has therefore emerged as an attractive target for anticancer drug discovery. Crystal structures of human LDH-A in the presence of inhibitors have been described, but currently no structures of the apo or binary NADH-bound forms are available for any mammalian LDH-A. Here, the apo structure of human LDH-A was solved at a resolution of 2.1 A in space group P4122. The active-site loop adopts an open conformation and the packing and crystallization conditions suggest that the crystal form is suitable for soaking experiments. The soaking potential was assessed with the cofactor NADH, which yielded a ligand-bound crystal structure in the absence of any inhibitors. The structures show that NADH binding induces small conformational changes in the active-site loop and an adjacent helix. A comparison with other eukaryotic apo LDH structures reveals the conservation of intra-loop interactions. The structures provide novel insight into cofactor binding and provide the foundation for soaking experiments with fragments and inhibitors.
		+
		+	Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase.,Dempster S, Harper S, Moses JE, Dreveny I Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1484-90. doi:, 10.1107/S1399004714005422. Epub 2014 Apr 30. PMID:24816116<ref>PMID:24816116</ref>
		+
		+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: L-lactate dehydrogenase]]		[[Category: L-lactate dehydrogenase]]
	[[Category: Dempster, S.]]		[[Category: Dempster, S.]]

OCA at 06:58, 7 May 2014

2014-05-07T06:58:49Z

←Older revision		Revision as of 06:58, 7 May 2014
Line 1:		Line 1:
-	==Structural ~~Characterisation~~ of the ~~Apo-form~~ of ~~Human Lactate Dehydrogenase~~ M ~~Isozyme~~==	+	==Structural characterisation of the NADH binary complex of human lactate dehydrogenase M isozyme==
	<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 09:27, 1 May 2014

2014-05-01T09:27:02Z

←Older revision		Revision as of 09:27, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[4l4s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L4S OCA]. <br>	+	<table><tr><td colspan='2'>[[4l4s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L4S OCA]. <br>
-	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene><br>
-	<b>[[Related_structure\|Related:]]</b> [[4l4r\|4l4r]]<br>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l4r\|4l4r]]</td></tr>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s PDBsum]</span><br>	+	<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=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s PDBsum]</span></td></tr>
		+	<table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[http://omim.org/entry/612933 612933]]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>		[[http://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[http://omim.org/entry/612933 612933]]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>

OCA at 09:57, 30 April 2014

2014-04-30T09:57:32Z

←Older revision		Revision as of 09:57, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[4l4s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L4S OCA]. <br>		[[4l4s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L4S OCA]. <br>
-	<b>Related:</b> [[4l4r\|4l4r]]<br>	+	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene><br>
		+	<b>[[Related_structure\|Related:]]</b> [[4l4r\|4l4r]]<br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l4s RCSB], [http://www.ebi.ac.uk/pdbsum/4l4s PDBsum]</span><br>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[http://omim.org/entry/612933 612933]]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>		[[http://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[http://omim.org/entry/612933 612933]]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>

OCA at 08:01, 30 April 2014

2014-04-30T08:01:50Z

←Older revision		Revision as of 08:01, 30 April 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Structural Characterisation of the Apo-form of Human Lactate Dehydrogenase M Isozyme==
		+	<StructureSection load='4l4s' size='340' side='right' caption='[[4l4s]], [[Resolution\|resolution]] 2.90Å' scene=''>
		+	== Structural highlights ==
		+	[[4l4s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L4S OCA]. <br>
		+	<b>Related:</b> [[4l4r\|4l4r]]<br>
		+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/LDHA_HUMAN LDHA_HUMAN]] Defects in LDHA are the cause of glycogen storage disease type 11 (GSD11) [MIM:[http://omim.org/entry/612933 612933]]. A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.<ref>PMID:2334430</ref>
		+	== Function ==

-	~~The entry 4l4s is ON HOLD until Paper Publication~~	+	== References ==
-		+	<references/>
-	~~Authors~~: Dempster, S., Harper, S., Moses, J.E.~~, Dreveny, I.~~	+	__TOC__
-		+	</StructureSection>
-	~~Description~~: ~~Structural Characterisation of the Apo-form of Human Lactate Dehydrogenase M Isozyme~~	+	[[Category: L-lactate dehydrogenase]]
		+	[[Category: Dempster, S.]]
		+	[[Category: Dreveny, I.]]
		+	[[Category: Harper, S.]]
		+	[[Category: Moses, J E.]]
		+	[[Category: Anaerobic respiration]]
		+	[[Category: Glycolysis]]
		+	[[Category: Oxidoreductase]]

OCA at 07:33, 15 January 2014

2014-01-15T07:33:22Z

←Older revision		Revision as of 07:33, 15 January 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4l4s is ON HOLD	+	The entry 4l4s is ON HOLD until Paper Publication

	Authors: Dempster, S., Harper, S., Moses, J.E., Dreveny, I.		Authors: Dempster, S., Harper, S., Moses, J.E., Dreveny, I.

	Description: Structural Characterisation of the Apo-form of Human Lactate Dehydrogenase M Isozyme		Description: Structural Characterisation of the Apo-form of Human Lactate Dehydrogenase M Isozyme