2oxd

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[[Image:2oxd.jpg|left|200px]]
 
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{{Structure
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==Protein kinase CK2 in complex with tetrabromobenzoimidazole K17, K22 and K32 inhibitors==
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|PDB= 2oxd |SIZE=350|CAPTION= <scene name='initialview01'>2oxd</scene>, resolution 2.30&Aring;
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<StructureSection load='2oxd' size='340' side='right'caption='[[2oxd]], [[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=K32:4,5,6,7-TETRABROMO-1H,3H-BENZIMIDAZOL-2-ONE'>K32</scene>
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<table><tr><td colspan='2'>[[2oxd]] 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=2OXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OXD 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=K32:4,5,6,7-TETRABROMO-1H,3H-BENZIMIDAZOL-2-ONE'>K32</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=2oxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxd OCA], [https://pdbe.org/2oxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oxd RCSB], [https://www.ebi.ac.uk/pdbsum/2oxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oxd ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1j91|1J91]], [[1zoh|1ZOH]], [[1zog|1ZOG]], [[1zoe|1ZOE]], [[2oxx|2OXX]], [[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=2oxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxd OCA], [http://www.ebi.ac.uk/pdbsum/2oxd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oxd 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/2oxd_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=2oxd 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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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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'''Protein kinase CK2 in complex with tetrabromobenzoimidazole K17, K22 and K32 inhibitors'''
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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:17768728<ref>PMID:17768728</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 2oxd" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[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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2OXD 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=2OXD OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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 complex]]
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[[Category: kinase]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:24:34 2008''
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Current revision

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

PDB ID 2oxd

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