1ZOH
Crystal structure of protein kinase CK2 in complex with TBB-derivatives inhibitors
Summary for 1ZOH
| Entry DOI | 10.2210/pdb1zoh/pdb |
| Related | 1ZOE 1ZOG |
| Descriptor | PROTEIN KINASE CK2, ALPHA SUBUNIT, SODIUM ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | protein kinase ck2, tetrabromo-benzimidazole, tbb, inhibitors, pharmacophore, transferase |
| Biological source | Zea mays |
| Total number of polymer chains | 1 |
| Total formula weight | 39935.93 |
| Authors | Battistutta, R.,Mazzorana, M.,Sarno, S.,Kazimierczuk, Z.,Zanotti, G.,Pinna, L.A. (deposition date: 2005-05-13, release date: 2005-11-29, Last modification date: 2024-02-14) |
| Primary citation | Battistutta, R.,Mazzorana, M.,Sarno, S.,Kazimierczuk, Z.,Zanotti, G.,Pinna, L.A. Inspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole. Chem.Biol., 12:1211-1219, 2005 Cited by PubMed Abstract: CK2 is a very pleiotropic protein kinase whose high constitutive activity is suspected to cooperate to neoplasia. Here, the crystal structure of the complexes between CK2 and three selective tetrabromo-benzimidazole derivatives inhibiting CK2 with Ki values between 40 and 400 nM are presented. The ligands bind to the CK2 active site in a different way with respect to the parent compound TBB. They enter more deeply into the cavity, establishing halogen bonds with the backbone of Glu114 and Val116 in the hinge region. A detailed analysis of the interactions highlights a major role of the hydrophobic effect in establishing the rank of potency within this class of inhibitors and shows that polar interactions are responsible for the different orientation of the molecules in the active site. PubMed: 16298300DOI: 10.1016/j.chembiol.2005.08.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
Download full validation report
