1qf8
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1qf8.png|left|200px]] | ||
- | < | + | ==TRUNCATED FORM OF CASEIN KINASE II BETA SUBUNIT (2-182) FROM HOMO SAPIENS== |
- | + | <StructureSection load='1qf8' size='340' side='right'caption='[[1qf8]], [[Resolution|resolution]] 1.74Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1qf8]] is a 2 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=1QF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QF8 FirstGlance]. <br> | |
- | or | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <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=1qf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qf8 OCA], [https://pdbe.org/1qf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qf8 RCSB], [https://www.ebi.ac.uk/pdbsum/1qf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qf8 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> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qf/1qf8_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qf8 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Protein kinase CK2 is a tetramer composed of two alpha catalytic subunits and two beta regulatory subunits. The structure of a C-terminal truncated form of the human beta subunit has been determined by X-ray crystallography to 1.7 A resolution. One dimer is observed in the asymmetric unit of the crystal. The most striking feature of the structure is the presence of a zinc finger mediating the dimerization. The monomer structure consists of two domains, one entirely alpha-helical and one including the zinc finger. The dimer has a crescent shape holding a highly acidic region at both ends. We propose that this acidic region is involved in the interactions with the polyamines and/or catalytic subunits. Interestingly, conserved amino acid residues among beta subunit sequences are clustered along one linear ridge that wraps around the entire dimer. This feature suggests that protein partners may interact with the dimer through a stretch of residues in an extended conformation. | ||
- | + | Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization.,Chantalat L, Leroy D, Filhol O, Nueda A, Benitez MJ, Chambaz EM, Cochet C, Dideberg O EMBO J. 1999 Jun 1;18(11):2930-40. PMID:10357806<ref>PMID:10357806</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 1qf8" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Casein kinase 3D structures|Casein kinase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Benitez | + | [[Category: Benitez MJ]] |
- | [[Category: Chambaz | + | [[Category: Chambaz E]] |
- | [[Category: Chantalat | + | [[Category: Chantalat L]] |
- | [[Category: Cochet | + | [[Category: Cochet C]] |
- | [[Category: Dideberg | + | [[Category: Dideberg O]] |
- | [[Category: Filhol | + | [[Category: Filhol O]] |
- | [[Category: Leroy | + | [[Category: Leroy D]] |
- | [[Category: Nueda | + | [[Category: Nueda A]] |
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Current revision
TRUNCATED FORM OF CASEIN KINASE II BETA SUBUNIT (2-182) FROM HOMO SAPIENS
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Categories: Homo sapiens | Large Structures | Benitez MJ | Chambaz E | Chantalat L | Cochet C | Dideberg O | Filhol O | Leroy D | Nueda A