1rqf

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[[Image:1rqf.gif|left|200px]]
 
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{{Structure
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==Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide==
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|PDB= 1rqf |SIZE=350|CAPTION= <scene name='initialview01'>1rqf</scene>, resolution 2.89&Aring;
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<StructureSection load='1rqf' size='340' side='right'caption='[[1rqf]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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<table><tr><td colspan='2'>[[1rqf]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQF FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.89&#8491;</td></tr>
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|GENE= KC2B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])
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<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>
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}}
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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=1rqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqf OCA], [https://pdbe.org/1rqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqf RCSB], [https://www.ebi.ac.uk/pdbsum/1rqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CSK2B_XENLA CSK2B_XENLA] Participates in Wnt signaling. Plays a complex role in regulating the basal catalytic activity of the alpha subunit (By similarity).
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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/rq/1rqf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1rqf 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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A truncated form of the regulatory subunit of the protein kinase CK2beta (residues 1-178) has been crystallized in the presence of a fragment of the cyclin-dependent kinase inhibitor p21WAF1 (residues 46-65) and the structure solved at 2.9 A resolution by molecular replacement. The core of the CK2beta dimer shows a high structural similarity with that identified in previous structural analyses of the dimer and the holoenzyme. However, the electron density corresponding to the substrate-binding acidic loop (residues 55-64) indicates two conformations that differ from that of the holoenzyme structure [Niefind et al. (2001), EMBO J. 20, 5320-5331]. Difference electron density near the dimerization region in each of the eight protomers in the asymmetric unit is attributed to between one and eight amino-acid residues of a complexed fragment of p21WAF1. This binding site corresponds to the solvent-accessible part of the conserved zinc-finger motif.
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'''Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide'''
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Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop.,Bertrand L, Sayed MF, Pei XY, Parisini E, Dhanaraj V, Bolanos-Garcia VM, Allende JE, Blundell TL Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1698-704. Epub, 2004 Sep 23. PMID:15388915<ref>PMID:15388915</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 1rqf" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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A truncated form of the regulatory subunit of the protein kinase CK2beta (residues 1-178) has been crystallized in the presence of a fragment of the cyclin-dependent kinase inhibitor p21WAF1 (residues 46-65) and the structure solved at 2.9 A resolution by molecular replacement. The core of the CK2beta dimer shows a high structural similarity with that identified in previous structural analyses of the dimer and the holoenzyme. However, the electron density corresponding to the substrate-binding acidic loop (residues 55-64) indicates two conformations that differ from that of the holoenzyme structure [Niefind et al. (2001), EMBO J. 20, 5320-5331]. Difference electron density near the dimerization region in each of the eight protomers in the asymmetric unit is attributed to between one and eight amino-acid residues of a complexed fragment of p21WAF1. This binding site corresponds to the solvent-accessible part of the conserved zinc-finger motif.
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*[[Casein kinase 3D structures|Casein kinase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1RQF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQF OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Homo sapiens]]
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Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop., Bertrand L, Sayed MF, Pei XY, Parisini E, Dhanaraj V, Bolanos-Garcia VM, Allende JE, Blundell TL, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1698-704. Epub, 2004 Sep 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15388915 15388915]
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[[Category: Large Structures]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Single protein]]
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[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Allende, J E.]]
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[[Category: Allende JE]]
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[[Category: Bertrand, L.]]
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[[Category: Bertrand L]]
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[[Category: Blundell, T L.]]
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[[Category: Blundell TL]]
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[[Category: Bolanos-Garcia, V M.]]
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[[Category: Bolanos-Garcia VM]]
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[[Category: Dhanaraj, V.]]
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[[Category: Dhanaraj V]]
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[[Category: Parisini, E.]]
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[[Category: Parisini E]]
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[[Category: Pei, X Y.]]
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[[Category: Pei X-Y]]
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[[Category: Sayed, M F.]]
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[[Category: Sayed MF]]
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[[Category: UNK]]
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[[Category: ZN]]
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[[Category: casein kinase beta subunit]]
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[[Category: cyclin-dependent kinase inhibitor]]
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[[Category: ser/thr protein kinase]]
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[[Category: zn finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:54:56 2008''
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Current revision

Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide

PDB ID 1rqf

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