View source for 6ttq


==PKM2 in complex with Compound 10==
<SX load='6ttq' size='340' side='right' viewer='molstar' caption='[[6ttq]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ttq]] 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=6TTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TTQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=NXH:1-propan-2-yl-3-pyridin-4-yl-urea'>NXH</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=6ttq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ttq OCA], [https://pdbe.org/6ttq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ttq RCSB], [https://www.ebi.ac.uk/pdbsum/6ttq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ttq ProSAT]</span></td></tr>
</table>
== 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> 
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== Publication Abstract from PubMed ==
Recent advances in cryo-electron microscopy (EM) structure determination have pushed the resolutions obtainable by the method into the range widely considered to be of utility for drug discovery. Here, we review the use of cryo-EM in fragment-based drug discovery (FBDD) based on in-house method development. We demonstrate not only that cryo-EM can reveal details of the molecular interactions between fragments and a protein, but also that the current reproducibility, quality, and throughput are compatible with FBDD. We exemplify this using the test system beta-galactosidase (Bgal) and the oncology target pyruvate kinase 2 (PKM2).

Fragment-based drug discovery using cryo-EM.,Saur M, Hartshorn MJ, Dong J, Reeks J, Bunkoczi G, Jhoti H, Williams PA Drug Discov Today. 2019 Dec 23. pii: S1359-6446(19)30465-9. doi:, 10.1016/j.drudis.2019.12.006. PMID:31877353<ref>PMID:31877353</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6ttq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
== References ==
<references/>
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</SX>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bunkoczi G]]
[[Category: Dong J]]
[[Category: Hartshorn MJ]]
[[Category: Jhoti H]]
[[Category: Reeks J]]
[[Category: Saur M]]
[[Category: Williams PA]]