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==rat LDHA in complex with 4-((2-allylsulfanyl-1,3-benzothizol-6-yl) amino)-4-oxo-butanoic acid== | ==rat LDHA in complex with 4-((2-allylsulfanyl-1,3-benzothizol-6-yl) amino)-4-oxo-butanoic acid== | ||
<StructureSection load='4aj4' size='340' side='right' caption='[[4aj4]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4aj4' size='340' side='right' caption='[[4aj4]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4aj4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4aj4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AJ4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=VAB:4-OXO-4-{[2-(PROP-2-EN-1-YLSULFANYL)-1,3-BENZOTHIAZOL-6-YL]AMINO}BUTANOIC+ACID'>VAB</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=VAB:4-OXO-4-{[2-(PROP-2-EN-1-YLSULFANYL)-1,3-BENZOTHIAZOL-6-YL]AMINO}BUTANOIC+ACID'>VAB</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4aj1|4aj1]], [[4aj2|4aj2]], [[4aje|4aje]], [[4ajh|4ajh]], [[4aji|4aji]], [[4ajj|4ajj]], [[4ajk|4ajk]], [[4ajl|4ajl]], [[4ajn|4ajn]], [[4ajo|4ajo]], [[4ajp|4ajp]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4aj1|4aj1]], [[4aj2|4aj2]], [[4aje|4aje]], [[4ajh|4ajh]], [[4aji|4aji]], [[4ajj|4ajj]], [[4ajk|4ajk]], [[4ajl|4ajl]], [[4ajn|4ajn]], [[4ajo|4ajo]], [[4ajp|4ajp]]</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=4aj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aj4 RCSB], [http://www.ebi.ac.uk/pdbsum/4aj4 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=4aj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aj4 OCA], [http://pdbe.org/4aj4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4aj4 RCSB], [http://www.ebi.ac.uk/pdbsum/4aj4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4aj4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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 4aj4" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Buffalo rat]] | |||
[[Category: L-lactate dehydrogenase]] | [[Category: L-lactate dehydrogenase]] | ||
[[Category: Brassington, C]] | [[Category: Brassington, C]] | ||
[[Category: Davies, G]] | [[Category: Davies, G]] | ||
Revision as of 15:34, 11 August 2016
rat LDHA in complex with 4-((2-allylsulfanyl-1,3-benzothizol-6-yl) amino)-4-oxo-butanoic acidrat LDHA in complex with 4-((2-allylsulfanyl-1,3-benzothizol-6-yl) amino)-4-oxo-butanoic acid
Structural highlights
Publication Abstract from PubMedLactate dehydrogenase A (LDHA) catalyzes the conversion of pyruvate to lactate, utilizing NADH as a cofactor. It has been identified as a potential therapeutic target in the area of cancer metabolism. In this manuscript we report our progress using fragment-based lead generation (FBLG), assisted by X-ray crystallography to develop small molecule LDHA inhibitors. Fragment hits were identified through NMR and SPR screening and optimized into lead compounds with nanomolar binding affinities via fragment linking. Also reported is their modification into cellular active compounds suitable for target validation work. Design and synthesis of novel lactate dehydrogenase a inhibitors by fragment-based lead generation.,Ward RA, Brassington C, Breeze AL, Caputo A, Critchlow S, Davies G, Goodwin L, Hassall G, Greenwood R, Holdgate GA, Mrosek M, Norman RA, Pearson S, Tart J, Tucker JA, Vogtherr M, Whittaker D, Wingfield J, Winter J, Hudson K J Med Chem. 2012 Apr 12;55(7):3285-306. Epub 2012 Mar 26. PMID:22417091[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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