4mpc
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mpc]] is a 1 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=4MPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MPC FirstGlance]. <br> | <table><tr><td colspan='2'>[[4mpc]] is a 1 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=4MPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MPC FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PV2:4-(ISOINDOLIN-2-YLSULFONYL)BENZENE-1,3-DIOL'>PV2</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PV2:4-(ISOINDOLIN-2-YLSULFONYL)BENZENE-1,3-DIOL'>PV2</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mp2|4mp2]], [[4mp7|4mp7]], [[4mpe|4mpe]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mp2|4mp2]], [[4mp7|4mp7]], [[4mpe|4mpe]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDK2, PDHK2 ([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">PDK2, PDHK2 ([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_dehydrogenase_(acetyl-transferring)]_kinase [Pyruvate dehydrogenase (acetyl-transferring)] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.2 2.7.11.2] </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_dehydrogenase_(acetyl-transferring)]_kinase [Pyruvate dehydrogenase (acetyl-transferring)] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.2 2.7.11.2] </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=4mpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mpc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mpc RCSB], [http://www.ebi.ac.uk/pdbsum/4mpc 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=4mpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mpc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mpc RCSB], [http://www.ebi.ac.uk/pdbsum/4mpc PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PDK2_HUMAN PDK2_HUMAN]] Serine/threonine kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis.<ref>PMID:7499431</ref> <ref>PMID:9787110</ref> <ref>PMID:17222789</ref> <ref>PMID:19833728</ref> <ref>PMID:21283817</ref> <ref>PMID:22123926</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Structure-guided Development of Specific Pyruvate Dehydrogenase Kinase Inhibitors Targeting the ATP-binding Pocket.,Tso SC, Qi X, Gui WJ, Wu CY, Chuang JL, Wernstedt-Asterholm I, Morlock LK, Owens KR, Scherer PE, Williams NS, Tambar UK, Wynn RM, Chuang DT J Biol Chem. 2013 Dec 19. PMID:24356970<ref>PMID:24356970</ref> | Structure-guided Development of Specific Pyruvate Dehydrogenase Kinase Inhibitors Targeting the ATP-binding Pocket.,Tso SC, Qi X, Gui WJ, Wu CY, Chuang JL, Wernstedt-Asterholm I, Morlock LK, Owens KR, Scherer PE, Williams NS, Tambar UK, Wynn RM, Chuang DT J Biol Chem. 2013 Dec 19. PMID:24356970<ref>PMID:24356970</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Pyruvate dehydrogenase kinase|Pyruvate dehydrogenase kinase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| - | [[Category: Chuang, D T | + | [[Category: Chuang, D T]] |
| - | [[Category: Chuang, J L | + | [[Category: Chuang, J L]] |
| - | [[Category: Gui, W J | + | [[Category: Gui, W J]] |
| - | [[Category: Qi, X | + | [[Category: Qi, X]] |
| - | [[Category: Tambar, U K | + | [[Category: Tambar, U K]] |
| - | [[Category: Tso, S C | + | [[Category: Tso, S C]] |
| - | [[Category: Wu, C Y | + | [[Category: Wu, C Y]] |
| - | [[Category: Wynn, R M | + | [[Category: Wynn, R M]] |
[[Category: Bergerat nucleotide-binding fold]] | [[Category: Bergerat nucleotide-binding fold]] | ||
[[Category: Cancer]] | [[Category: Cancer]] | ||
Revision as of 21:42, 25 December 2014
Crystal structure of pyruvate dehydrogenase kinase isoform 2 in complex with inhibitor PS2
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Categories: Human | Chuang, D T | Chuang, J L | Gui, W J | Qi, X | Tambar, U K | Tso, S C | Wu, C Y | Wynn, R M | Bergerat nucleotide-binding fold | Cancer | Ghkl protein kinase | Hepatic steatosis | Impaired glucose oxidation | Mitochondrial protein kinase | Protein kinase | Pyruvate dehydrogenase complex | Transferase-transferase inhibitor complex | Type 2 diabetes
