2oxx

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[[Image:2oxx.jpg|left|200px]]
 
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{{Structure
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==Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32==
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|PDB= 2oxx |SIZE=350|CAPTION= <scene name='initialview01'>2oxx</scene>, resolution 2.30&Aring;
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<StructureSection load='2oxx' size='340' side='right'caption='[[2oxx]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=K22:4,5,6,7-TETRABROMO-1H,3H-BENZIMIDAZOL-2-THIONE'>K22</scene>
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<table><tr><td colspan='2'>[[2oxx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OXX FirstGlance]. <br>
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|ACTIVITY= <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>
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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]] 2.3&#8491;</td></tr>
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|GENE= ACK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 Zea mays])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K22:4,5,6,7-TETRABROMO-1H,3H-BENZIMIDAZOL-2-THIONE'>K22</scene></td></tr>
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|DOMAIN=
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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=2oxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxx OCA], [https://pdbe.org/2oxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oxx RCSB], [https://www.ebi.ac.uk/pdbsum/2oxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oxx ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1j91|1J91]], [[1zoh|1ZOH]], [[1zog|1ZOG]], [[1zoe|1ZOE]], [[2oxd|2OXD]], [[2oxy|2OXY]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxx OCA], [http://www.ebi.ac.uk/pdbsum/2oxx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oxx RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CSK2A_MAIZE CSK2A_MAIZE] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.
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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/ox/2oxx_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=2oxx ConSurf].
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<div style="clear:both"></div>
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'''Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32'''
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==See Also==
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*[[Casein kinase 3D structures|Casein kinase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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CK2 is a highly pleiotropic Ser/Thr protein kinase that is able to promote cell survival and enhance the tumour phenotype under specific circumstances. We have determined the crystal structure of three new complexes with tetrabromobenzimidazole derivatives that display K(i) values between 0.15 and 0.30 microM. A comparative analysis of these data with those of four other inhibitors of the same family revealed the presence of some highly conserved water molecules in the ATP-binding site. These waters reside near Lys68, in an area with a positive electrostatic potential that is able to attract and orient negatively charged ligands. The presence of this positive region and two unique bulky residues that are typical of CK2, Ile66 and Ile174, play a critical role in determining the ligand orientation and binding selectivity.
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[[Category: Large Structures]]
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==About this Structure==
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2OXX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXX OCA].
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==Reference==
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The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules., Battistutta R, Mazzorana M, Cendron L, Bortolato A, Sarno S, Kazimierczuk Z, Zanotti G, Moro S, Pinna LA, Chembiochem. 2007 Oct 15;8(15):1804-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17768728 17768728]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Single protein]]
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[[Category: Zea mays]]
[[Category: Zea mays]]
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[[Category: Battistutta, R.]]
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[[Category: Battistutta R]]
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[[Category: Cendron, L.]]
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[[Category: Cendron L]]
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[[Category: Zanotti, G.]]
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[[Category: Zanotti G]]
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[[Category: inhibitor]]
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[[Category: protein kinase ck2]]
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[[Category: tetrabromobenzoimidazole derivative]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:24:52 2008''
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Current revision

Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32

PDB ID 2oxx

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