2oxd

From Proteopedia

(Difference between revisions)

Revision as of 07:03, 10 September 2015

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

Structural highlights

2oxd is a 1 chain structure with sequence from Maize. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1j91, 1zoh, 1zog, 1zoe, 2oxx, 2oxy
Gene:	ACK2 (MAIZE)
Activity:	Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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.

Publication Abstract from PubMed

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.

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^[1]

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

References

↑ Battistutta R, Mazzorana M, Cendron L, Bortolato A, Sarno S, Kazimierczuk Z, Zanotti G, Moro S, Pinna LA. The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules. Chembiochem. 2007 Oct 15;8(15):1804-9. PMID:17768728 doi:10.1002/cbic.200700307

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2oxd"

@@ Line 2: / Line 2: @@
 <StructureSection load='2oxd' size='340' side='right' caption='[[2oxd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2oxd]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OXD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2oxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Maize Maize]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OXD FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K32:4,5,6,7-TETRABROMO-1H,3H-BENZIMIDAZOL-2-ONE'>K32</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j91|1j91]], [[1zoh|1zoh]], [[1zog|1zog]], [[1zoe|1zoe]], [[2oxx|2oxx]], [[2oxy|2oxy]]</td></tr>
-<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>
+<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 MAIZE])</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=2oxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2oxd RCSB], [http://www.ebi.ac.uk/pdbsum/2oxd PDBsum]</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=2oxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxd OCA], [http://pdbe.org/2oxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oxd RCSB], [http://www.ebi.ac.uk/pdbsum/2oxd PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2oxd" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
+[[Category: Maize]]
 [[Category: Non-specific serine/threonine protein kinase]]
-[[Category: Zea mays]]
 [[Category: Battistutta, R]]
 [[Category: Cendron, L]]

2oxd

From Proteopedia

Revision as of 07:03, 10 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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