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| | ==Crystal Structure of full-length symmetric CK2 holoenzyme== | | ==Crystal Structure of full-length symmetric CK2 holoenzyme== |
| - | <StructureSection load='4md7' size='340' side='right' caption='[[4md7]], [[Resolution|resolution]] 3.10Å' scene=''> | + | <StructureSection load='4md7' size='340' side='right'caption='[[4md7]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4md7]] is a 8 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=4MD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MD7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4md7]] is a 8 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=4MD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MD7 FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4md8|4md8]], [[4md9|4md9]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CSNK2B, CK2N, G5A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CSNK2A1, CK2A1 ([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=4md7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4md7 OCA], [https://pdbe.org/4md7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4md7 RCSB], [https://www.ebi.ac.uk/pdbsum/4md7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4md7 ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
| + | </table> |
| - | <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=4md7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4md7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4md7 RCSB], [http://www.ebi.ac.uk/pdbsum/4md7 PDBsum]</span></td></tr> | + | == Function == |
| - | <table> | + | [https://www.uniprot.org/uniprot/CSK2B_HUMAN CSK2B_HUMAN] Participates in Wnt signaling (By similarity). Plays a complex role in regulating the basal catalytic activity of the alpha subunit.<ref>PMID:11239457</ref> <ref>PMID:16818610</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | Active Form of the Protein Kinase CK2 alphabeta Holoenzyme Is a Strong Complex with Symmetric Architecture.,Lolli G, Ranchio A, Battistutta R ACS Chem Biol. 2013 Nov 11. PMID:24175891<ref>PMID:24175891</ref> | | Active Form of the Protein Kinase CK2 alphabeta Holoenzyme Is a Strong Complex with Symmetric Architecture.,Lolli G, Ranchio A, Battistutta R ACS Chem Biol. 2013 Nov 11. PMID:24175891<ref>PMID:24175891</ref> |
| | | | |
| - | 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 4md7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Casein kinase 3D structures|Casein kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Non-specific serine/threonine protein kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Battistutta, R.]] | + | [[Category: Battistutta R]] |
| - | [[Category: Lolli, G.]] | + | [[Category: Lolli G]] |
| - | [[Category: Ranchio, A.]] | + | [[Category: Ranchio A]] |
| - | [[Category: Protein serine/threonine kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
CSK2B_HUMAN Participates in Wnt signaling (By similarity). Plays a complex role in regulating the basal catalytic activity of the alpha subunit.[1] [2]
Publication Abstract from PubMed
CK2 is a protein kinase essential for cell viability whose activity is altered in several cancers. Its mechanisms of regulation differ from those common to other eukaryotic protein kinases and are not entirely established yet. Here we present crystal structures of the monomeric form of the alpha2beta2 holoenzyme that allow refining a formerly proposed structural model for activity regulation by oligomerization. Previous crystal structures of the CK2 holoenzyme show an asymmetric arrangement of the two alpha catalytic subunits around the obligate beta2 regulatory subunits. Asymmetric alpha2beta2 tetramers are organized in trimeric rings that correspond to inactive forms of the enzyme. The new crystal structures presented here reveal the symmetric architecture of the isolated active tetramers. The dimension and the nature of the alpha/beta interfaces configure the holoenzyme as a strong complex that does not spontaneously dissociate in solution, in accordance with the low dissociation constant ( approximately 4 nM).
Active Form of the Protein Kinase CK2 alphabeta Holoenzyme Is a Strong Complex with Symmetric Architecture.,Lolli G, Ranchio A, Battistutta R ACS Chem Biol. 2013 Nov 11. PMID:24175891[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Keller DM, Zeng X, Wang Y, Zhang QH, Kapoor M, Shu H, Goodman R, Lozano G, Zhao Y, Lu H. A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Mol Cell. 2001 Feb;7(2):283-92. PMID:11239457
- ↑ Cheusova T, Khan MA, Schubert SW, Gavin AC, Buchou T, Jacob G, Sticht H, Allende J, Boldyreff B, Brenner HR, Hashemolhosseini S. Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction. Genes Dev. 2006 Jul 1;20(13):1800-16. PMID:16818610 doi:http://dx.doi.org/10.1101/gad.375206
- ↑ Lolli G, Ranchio A, Battistutta R. Active Form of the Protein Kinase CK2 alphabeta Holoenzyme Is a Strong Complex with Symmetric Architecture. ACS Chem Biol. 2013 Nov 11. PMID:24175891 doi:http://dx.doi.org/10.1021/cb400771y
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