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3pvg

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==Crystal structure of Z. mays CK2 alpha subunit in complex with the inhibitor 4,5,6,7-tetrabromo-1-carboxymethylbenzimidazole (K68)==
==Crystal structure of Z. mays CK2 alpha subunit in complex with the inhibitor 4,5,6,7-tetrabromo-1-carboxymethylbenzimidazole (K68)==
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<StructureSection load='3pvg' size='340' side='right' caption='[[3pvg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='3pvg' size='340' side='right'caption='[[3pvg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pvg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3kxj 3kxj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PVG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pvg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3kxj 3kxj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PVG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K68:(4,5,6,7-TETRABROMO-1H-BENZIMIDAZOL-1-YL)ACETIC+ACID'>K68</scene></td></tr>
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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]] 1.5&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=K68:(4,5,6,7-TETRABROMO-1H-BENZIMIDAZOL-1-YL)ACETIC+ACID'>K68</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 Zea mays])</td></tr>
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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=3pvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvg OCA], [https://pdbe.org/3pvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pvg RCSB], [https://www.ebi.ac.uk/pdbsum/3pvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pvg ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pvg RCSB], [http://www.ebi.ac.uk/pdbsum/3pvg PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CK2 denotes a pleiotropic, constitutively active protein kinase whose abnormally high level in many cancer cells is held as an example of "non oncogene addiction". A wide spectrum of cell permeable, fairly specific ATP site-directed CK2 inhibitors are currently available which are proving useful to dissect its biological functions and which share the property of inducing apoptosis of cancer cells with no comparable effect on their "normal" counterparts. One of these, CX-4945, has recently entered clinical trials for the treatment of advanced solid tumors, Castelman's disease and multiple myeloma. The solution of a wide range of 3D structures of inhibitors bound to the catalytic subunits of CK2 reveals that their efficacy substantially relies on hydrophobic interactions within a cavity which is smaller than in other protein kinases. Accordingly the potency of tetra-halogenated benzimidazoles increases upon replacement of chlorine by bromine and, even more, by iodine, and decreases if two unique bulky side chains on CK2 (Val66 and Ile174) are mutated to alanines. Many CK2 inhibitors have been tested on a panel of more than 60 kinases providing Promiscuity Scores useful to evaluate their selectivity, the lowest value (9.47), denoting highest selectivity, being displayed by quinalizarin. The observation that CK2 inhibitors with medium/high promiscuity scores share the ability to inhibit a group of protein kinases as effectively as CK2 discloses the possibility of using their scaffolds for the rational development of selective inhibitors of these kinases, with special reference to PIMs, DYRKs, HIPK2, PKD and ERK8.
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Atp Site-Directed Inhibitors of Protein Kinase Ck2: An Update.,Sarno S, Papinutto E, Franchin C, Bain J, Elliott M, Meggio F, Kazimierczuk Z, Orzeszko A, Zanotti G, Battistutta R, Pinna LA Curr Top Med Chem. 2011 Mar 29. PMID:21513497<ref>PMID:21513497</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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==See Also==
==See Also==
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*[[Casein kinase|Casein kinase]]
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*[[Casein kinase 3D structures|Casein kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
[[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: Franchin, C]]
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[[Category: Franchin C]]
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[[Category: Papinutto, E]]
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[[Category: Papinutto E]]
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[[Category: Protein kinase ck2-inhibitor complex]]
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[[Category: Transferase-transferase inhibitor complex]]
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Current revision

Crystal structure of Z. mays CK2 alpha subunit in complex with the inhibitor 4,5,6,7-tetrabromo-1-carboxymethylbenzimidazole (K68)

PDB ID 3pvg

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