2OXY

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

Summary for 2OXY

• Entry DOI: 10.2210/pdb2oxy/pdb
• Related: 1j91 1zoe 1zog 1zoh 2OXD 2OXX
• Descriptor: Casein kinase II subunit alpha, 4,5,6,7-TETRABROMO-BENZIMIDAZOLE (3 entities in total)
• Functional Keywords: protein kinase ck2, inhibitors, tetrabromobenzoimidazole derivatives, transferase
• Biological source: Zea mays
• Total number of polymer chains: 2
• Total formula weight: 79449.77

Authors

Battistutta, R.,Zanotti, G.,Cendron, L. (deposition date: 2007-02-21, release date: 2007-09-25, Last modification date: 2024-02-21)

Primary citation

Battistutta, R.,Mazzorana, M.,Cendron, L.,Bortolato, A.,Sarno, S.,Kazimierczuk, Z.,Zanotti, G.,Moro, S.,Pinna, L.A.
The ATP-Binding Site of Protein Kinase CK2 Holds a Positive Electrostatic Area and Conserved Water Molecules.
Chembiochem, 8:1804-1809, 2007

PubMed 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.

PubMed: 17768728
DOI: 10.1002/cbic.200700307

Experimental method

X-RAY DIFFRACTION (1.812 Å)