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[[Image:2oxy.jpg|left|200px]]


{{Structure
==Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32==
|PDB= 2oxy |SIZE=350|CAPTION= <scene name='initialview01'>2oxy</scene>, resolution 1.812&Aring;
<StructureSection load='2oxy' size='340' side='right'caption='[[2oxy]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=K17:4,5,6,7-TETRABROMO-BENZIMIDAZOLE'>K17</scene>
<table><tr><td colspan='2'>[[2oxy]] is a 2 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=2OXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OXY FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.812&#8491;</td></tr>
|GENE= ACK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 Zea mays])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K17:4,5,6,7-TETRABROMO-BENZIMIDAZOLE'>K17</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxy OCA], [https://pdbe.org/2oxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oxy RCSB], [https://www.ebi.ac.uk/pdbsum/2oxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oxy ProSAT]</span></td></tr>
|RELATEDENTRY=[[1j91|1J91]], [[1zoh|1ZOH]], [[1zog|1ZOG]], [[1zoe|1ZOE]], [[2oxd|2OXD]], [[2oxx|2OXX]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxy OCA], [http://www.ebi.ac.uk/pdbsum/2oxy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oxy RCSB]</span>
== Function ==
}}
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/2oxy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2oxy ConSurf].
<div style="clear:both"></div>


'''Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32'''
==See Also==
 
*[[Casein kinase 3D structures|Casein kinase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
2OXY 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=2OXY OCA].
 
==Reference==
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]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Single protein]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Battistutta, R.]]
[[Category: Battistutta R]]
[[Category: Cendron, L.]]
[[Category: Cendron L]]
[[Category: Zanotti, G.]]
[[Category: Zanotti G]]
[[Category: inhibitor]]
[[Category: protein kinase ck2]]
[[Category: tetrabromobenzoimidazole derivative]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:24:52 2008''

Latest revision as of 12:06, 21 February 2024

Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32

Structural highlights

2oxy is a 2 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.812Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2oxy, resolution 1.81Å

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