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{{STRUCTURE_3war| PDB=3war | SCENE= }}
==Crystal structure of human CK2a==
===Crystal structure of human CK2a===
<StructureSection load='3war' size='340' side='right' caption='[[3war]], [[Resolution|resolution]] 1.04&Aring;' scene=''>
{{ABSTRACT_PUBMED_24121351}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3war]] is a 1 chain structure with 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=3WAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WAR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NIO:NICOTINIC+ACID'>NIO</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<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>
<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=3war FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3war OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3war RCSB], [http://www.ebi.ac.uk/pdbsum/3war PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Ser/Thr kinase CK2 consists of two catalytic subunits (CK2alpha) and a dimer of the regulatory subunits (CK2beta), and is a ubiquitous enzyme that regulates growth, proliferation and the survival of cells. CK2 is a remarkable drug target for potentially treating a wide variety of tumours and glomerulonephritis. The purified CK2alpha protein was crystallized using ethylene glycol as a precipitant. The crystal structure of CK2alpha with 21 loci of alternative conformations, including a niacin, 19 ethylene glycols and 346 waters, was determined at 1.06 A resolution to an Rwork of 14.0% (Rfree = 16.5%). The alternative ensemble in the internal hydrophobic core underpins the plasticity of the alphaD-helix responsible for the regulation of ATP/GTP binding. The clear density map indicates that a niacin molecule, contained in the Escherichia coli culture medium, binds to the ATP binding site. An ethylene glycol molecule binds in the hydrophobic pocket lateral to the alphaD-helix forming the rim of the active site. The other ethylene glycol molecules occupy physiologically significant sites, including the CK2beta binding interface and substrate binding site, as well as the gap in the crystal packing. Together with water molecules in the active site, these structural insights should facilitate drug discovery.


==Function==
Crystal structure of human CK2alpha at 1.06 A resolution.,Kinoshita T, Nakaniwa T, Sekiguchi Y, Sogabe Y, Sakurai A, Nakamura S, Nakanishi I J Synchrotron Radiat. 2013 Nov;20(Pt 6):974-9. doi: 10.1107/S0909049513020785., Epub 2013 Oct 2. PMID:24121351<ref>PMID:24121351</ref>
[[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3war]] is a 1 chain structure with 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=3WAR OCA].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:024121351</ref><references group="xtra"/><references/>
*[[Casein kinase|Casein kinase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Kinoshita, T.]]
[[Category: Kinoshita, T]]
[[Category: Nakamura, S.]]
[[Category: Nakamura, S]]
[[Category: Nakanishi, I.]]
[[Category: Nakanishi, I]]
[[Category: Nakaniwa, T.]]
[[Category: Nakaniwa, T]]
[[Category: Sakurai, A.]]
[[Category: Sakurai, A]]
[[Category: Sekiguchi, Y.]]
[[Category: Sekiguchi, Y]]
[[Category: Sogabe, Y.]]
[[Category: Sogabe, Y]]
[[Category: Protein kinase]]
[[Category: Protein kinase]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 12:35, 21 December 2014

Crystal structure of human CK2aCrystal structure of human CK2a

Structural highlights

3war is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:CSNK2A1, CK2A1 (Homo sapiens)
Activity:Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

The Ser/Thr kinase CK2 consists of two catalytic subunits (CK2alpha) and a dimer of the regulatory subunits (CK2beta), and is a ubiquitous enzyme that regulates growth, proliferation and the survival of cells. CK2 is a remarkable drug target for potentially treating a wide variety of tumours and glomerulonephritis. The purified CK2alpha protein was crystallized using ethylene glycol as a precipitant. The crystal structure of CK2alpha with 21 loci of alternative conformations, including a niacin, 19 ethylene glycols and 346 waters, was determined at 1.06 A resolution to an Rwork of 14.0% (Rfree = 16.5%). The alternative ensemble in the internal hydrophobic core underpins the plasticity of the alphaD-helix responsible for the regulation of ATP/GTP binding. The clear density map indicates that a niacin molecule, contained in the Escherichia coli culture medium, binds to the ATP binding site. An ethylene glycol molecule binds in the hydrophobic pocket lateral to the alphaD-helix forming the rim of the active site. The other ethylene glycol molecules occupy physiologically significant sites, including the CK2beta binding interface and substrate binding site, as well as the gap in the crystal packing. Together with water molecules in the active site, these structural insights should facilitate drug discovery.

Crystal structure of human CK2alpha at 1.06 A resolution.,Kinoshita T, Nakaniwa T, Sekiguchi Y, Sogabe Y, Sakurai A, Nakamura S, Nakanishi I J Synchrotron Radiat. 2013 Nov;20(Pt 6):974-9. doi: 10.1107/S0909049513020785., Epub 2013 Oct 2. PMID:24121351[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Kinoshita T, Nakaniwa T, Sekiguchi Y, Sogabe Y, Sakurai A, Nakamura S, Nakanishi I. Crystal structure of human CK2alpha at 1.06 A resolution. J Synchrotron Radiat. 2013 Nov;20(Pt 6):974-9. doi: 10.1107/S0909049513020785., Epub 2013 Oct 2. PMID:24121351 doi:http://dx.doi.org/10.1107/S0909049513020785

3war, resolution 1.04Å

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