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PDBsum entry 2oxd
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protein ligands links
Transferase PDB id
2oxd

 

 

 

 

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Contents
Protein chain
325 a.a. *
Ligands
K32
Waters ×79
* Residue conservation analysis
PDB id:
2oxd
Name: Transferase
Title: Protein kinase ck2 in complex with tetrabromobenzoimidazole k17, k22 and k32 inhibitors
Structure: Casein kinase ii subunit alpha. Chain: a. Synonym: ck ii, ck2-alpha. Engineered: yes
Source: Zea mays. Organism_taxid: 4577. Gene: ack2. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.30Å     R-factor:   0.223     R-free:   0.273
Authors: R.Battistutta,G.Zanotti,L.Cendron
Key ref: R.Battistutta et al. (2007). The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules. Chembiochem, 8, 1804-1809. PubMed id: 17768728 DOI: 10.1002/cbic.200700307
Date:
20-Feb-07     Release date:   25-Sep-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P28523  (CSK2A_MAIZE) -  Casein kinase II subunit alpha from Zea mays
Seq:
Struc: 		332 a.a.
325 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
 + ATP
 = O-phospho-L-seryl-[protein]
 + ADP
 + H(+)
L-threonyl-[protein]
 + ATP
 = O-phospho-L-threonyl-[protein]
 + ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1002/cbic.200700307 Chembiochem 8:1804-1809 (2007)
PubMed id: 17768728  
 
 
The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules.
R.Battistutta, M.Mazzorana, L.Cendron, A.Bortolato, S.Sarno, Z.Kazimierczuk, G.Zanotti, S.Moro, L.A.Pinna.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19526464 G.Cozza, A.Bortolato, and S.Moro (2010).
How druggable is protein kinase CK2?
  Med Res Rev, 30, 419-462.  
19821123 N.Zhang, and R.Zhong (2010).
Structural basis for decreased affinity of Emodin binding to Val66-mutated human CK2 alpha as determined by molecular dynamics.
  J Mol Model, 16, 771-780.  
19432557 G.Cozza, M.Mazzorana, E.Papinutto, J.Bain, M.Elliott, G.di Maira, A.Gianoncelli, M.A.Pagano, S.Sarno, M.Ruzzene, R.Battistutta, F.Meggio, S.Moro, G.Zagotto, and L.A.Pinna (2009).
Quinalizarin as a potent, selective and cell-permeable inhibitor of protein kinase CK2.
  Biochem J, 421, 387-395.
PDB code: 3fl5
18548199 M.Bretner, A.Najda-Bernatowicz, M.Łebska, G.Muszyńska, A.Kilanowicz, and A.Sapota (2008).
New inhibitors of protein kinase CK2, analogues of benzimidazole and benzotriazole.
  Mol Cell Biochem, 316, 87-89.  
18704226 S.Sarno, and L.A.Pinna (2008).
Protein kinase CK2 as a druggable target.
  Mol Biosyst, 4, 889-894.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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