4md9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of symmetric CK2 holoenzyme with mutated alpha subunit (F121E truncated at aa 336)== | |
| + | <StructureSection load='4md9' size='340' side='right'caption='[[4md9]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4md9]] is a 16 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=4MD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MD9 FirstGlance]. <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]] 3.5Å</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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4md9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4md9 OCA], [https://pdbe.org/4md9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4md9 RCSB], [https://www.ebi.ac.uk/pdbsum/4md9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4md9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == 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<ref>PMID:24175891</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4md9" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Casein kinase 3D structures|Casein kinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Battistutta R]] | ||
| + | [[Category: Lolli G]] | ||
| + | [[Category: Ranchio A]] | ||
Current revision
Crystal Structure of symmetric CK2 holoenzyme with mutated alpha subunit (F121E truncated at aa 336)
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