6GIH
Crystal Structure of CK2alpha with CAM187 bound
Summary for 6GIH
| Entry DOI | 10.2210/pdb6gih/pdb |
| Descriptor | Casein kinase II subunit alpha, ACETATE ION, [3-chloranyl-5-(1~{H}-indol-4-yl)phenyl]methanamine, ... (4 entities in total) |
| Functional Keywords | ck2alpha, ck2a, fragment based drug discovery, high concentration screening, selective atp competitive inhibitors, surface entrophy reduction, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 39406.21 |
| Authors | Brear, P.,Iegre, J.,North, A.,De Fusco, C.,Georgiou, K.,Lubin, A.,Carro, L.,Sore, H.,Hyvonen, M.,Spring, D. (deposition date: 2018-05-11, release date: 2018-05-23, Last modification date: 2024-01-17) |
| Primary citation | Brear, P.,North, A.,Iegre, J.,Hadje Georgiou, K.,Lubin, A.,Carro, L.,Green, W.,Sore, H.F.,Hyvonen, M.,Spring, D.R. Novel non-ATP competitive small molecules targeting the CK2 alpha / beta interface. Bioorg. Med. Chem., 26:3016-3020, 2018 Cited by PubMed Abstract: Increased CK2 levels are prevalent in many cancers. Combined with the critical role CK2 plays in many cell-signaling pathways, this makes it a prime target for down regulation to fight tumour growth. Herein, we report a fragment-based approach to inhibiting the interaction between CK2α and CK2β at the α-β interface of the holoenzyme. A fragment, CAM187, with an IC of 44 μM and a molecular weight of only 257 gmol has been identified as the most promising compound. Importantly, the lead fragment only bound at the interface and was not observed in the ATP binding site of the protein when co-crystallised with CK2α. The fragment-like molecules discovered in this study represent unique scaffolds to CK2 inhibition and leave room for further optimisation. PubMed: 29759799DOI: 10.1016/j.bmc.2018.05.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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