2QC6
Protein kinase CK2 in complex with DBC
Summary for 2QC6
| Entry DOI | 10.2210/pdb2qc6/pdb |
| Descriptor | Casein kinase II subunit alpha, 3,8-DIBROMO-7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE (3 entities in total) |
| Functional Keywords | ck2, dbc, kinase inhibitors, coumarins, transferase |
| Biological source | Zea mays |
| Total number of polymer chains | 1 |
| Total formula weight | 39641.13 |
| Authors | Battistutta, R. (deposition date: 2007-06-19, release date: 2008-02-26, Last modification date: 2011-07-13) |
| Primary citation | Chilin, A.,Battistutta, R.,Bortolato, A.,Cozza, G.,Zanatta, S.,Poletto, G.,Mazzorana, M.,Zagotto, G.,Uriarte, E.,Guiotto, A.,Pinna, L.A.,Meggio, F.,Moro, S. Coumarin as attractive casein kinase 2 (CK2) inhibitor scaffold: an integrate approach to elucidate the putative binding motif and explain structure-activity relationships. J.Med.Chem., 51:752-759, 2008 Cited by PubMed Abstract: Casein kinase 2 (CK2) is an ubiquitous, essential, and highly pleiotropic protein kinase whose abnormally high constitutive activity is suspected to underlie its pathogenic potential in neoplasia and other diseases. Recently, using different virtual screening approaches, we have identified several novel CK2 inhibitors. In particular, we have discovered that coumarin moiety can be considered an attractive CK2 inhibitor scaffold. In the present work, we have synthetized and tested a small library of coumarins (more than 60), rationalizing the observed structure-activity relationship. Moreover, the most promising inhibitor, 3,8-dibromo-7-hydroxy-4-methylchromen-2-one (DBC), has been also crystallized in complex with CK2, and the experimental binding mode has been used to derive a linear interaction energy (LIE) model. PubMed: 18251491DOI: 10.1021/jm070909t PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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