3eed

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{{Seed}}
 
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[[Image:3eed.png|left|200px]]
 
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==Crystal structure of human protein kinase CK2 regulatory subunit (CK2beta; mutant 1-193)==
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The line below this paragraph, containing "STRUCTURE_3eed", creates the "Structure Box" on the page.
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<StructureSection load='3eed' size='340' side='right'caption='[[3eed]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3eed]] 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=3EED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EED FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3eed| PDB=3eed | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eed OCA], [https://pdbe.org/3eed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eed RCSB], [https://www.ebi.ac.uk/pdbsum/3eed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eed ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ee/3eed_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3eed ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The protein kinase CK2 (former name: "casein kinase 2") predominantly occurs as a heterotetrameric holoenzyme composed of two catalytic chains (CK2alpha) and two noncatalytic subunits (CK2beta). The CK2beta subunits form a stable dimer to which the CK2alpha monomers are attached independently. In contrast to the cyclins in the case of the cyclin-dependent kinases CK2beta is no on-switch of CK2alpha; rather the formation of the CK2 holoenzyme is accompanied with an overall change of the enzyme's profile including a modulation of the substrate specificity, an increase of the thermostability, and an allocation of docking sites for membranes and other proteins. In this study we used C-terminal deletion variants of human CK2alpha and CK2beta that were enzymologically fully competent and in particular able to form a heterotetrameric holoenzyme. With differential scanning calorimetry (DSC) we confirmed the strong thermostabilization effect of CK2alpha on CK2beta with an upshift of the CK2alpha melting temperature of more than 9 degrees . Using isothermal titration calorimetry (ITC) we measured a dissociation constant of 12.6 nM. This high affinity between CK2alpha and CK2beta is mainly caused by enthalpic rather than entropic contributions. Finally, we determined a crystal structure of the CK2beta construct to 2.8 A resolution and revealed by structural comparisons with the CK2 holoenzyme structure that the CK2beta conformation is largely conserved upon association with CK2alpha, whereas the latter undergoes significant structural adaptations of its backbone.
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===Crystal structure of human protein kinase CK2 regulatory subunit (CK2beta; mutant 1-193)===
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The interaction of CK2alpha and CK2beta, the subunits of protein kinase CK2, requires CK2beta in a preformed conformation and is enthalpically driven.,Raaf J, Brunstein E, Issinger OG, Niefind K Protein Sci. 2008 Dec;17(12):2180-6. Epub 2008 Sep 29. PMID:18824508<ref>PMID:18824508</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3eed" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18824508}}, adds the Publication Abstract to the page
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*[[Casein kinase 3D structures|Casein kinase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18824508 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18824508}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3EED is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EED OCA].
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==Reference==
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The interaction of CK2alpha and CK2beta, the subunits of protein kinase CK2, requires CK2beta in a preformed conformation and is enthalpically driven., Raaf J, Brunstein E, Issinger OG, Niefind K, Protein Sci. 2008 Dec;17(12):2180-6. Epub 2008 Sep 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18824508 18824508]
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Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme., Niefind K, Guerra B, Ermakowa I, Issinger OG, EMBO J. 2001 Oct 1;20(19):5320-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11574463 11574463]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
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[[Category: Issinger O-G]]
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[[Category: Casein kinase 2]]
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[[Category: Niefind K]]
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[[Category: Casein kinase ii]]
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[[Category: Raaf J]]
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[[Category: Eukaryotic protein kinase]]
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[[Category: Phosphoprotein]]
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[[Category: Protein kinase ck2]]
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[[Category: Transferase]]
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[[Category: Wnt signaling pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 3 20:36:05 2008''
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Current revision

Crystal structure of human protein kinase CK2 regulatory subunit (CK2beta; mutant 1-193)

PDB ID 3eed

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