4DGL
Crystal Structure of the CK2 Tetrameric Holoenzyme
Summary for 4DGL
| Entry DOI | 10.2210/pdb4dgl/pdb |
| Related | 1JWH |
| Descriptor | Casein kinase II subunit beta, Casein kinase II subunit alpha, ZINC ION, ... (4 entities in total) |
| Functional Keywords | protein kinase, transferase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 130191.17 |
| Authors | Lolli, G.,Battistutta, R. (deposition date: 2012-01-26, release date: 2012-05-02, Last modification date: 2024-02-28) |
| Primary citation | Lolli, G.,Pinna, L.A.,Battistutta, R. Structural determinants of protein kinase CK2 regulation by autoinhibitory polymerization. Acs Chem.Biol., 7:1158-1163, 2012 Cited by PubMed Abstract: CK2 is a Ser/Thr protein kinase essential for cell viability whose activity is anomalously high in several cancers. CK2 is a validated target for cancer therapy with one small molecule inhibitor in phase I clinical trials. This enzyme is not regulated by mechanisms common to other protein kinases, and how its activity is controlled is still unclear. We present a new crystal structure of the CK2 holoenzyme that supports an autoinhibitory mechanism of regulation whereby the β-subunit plays an essential role in the formation of inactive polymeric assemblies. The derived structural model of (down)regulation by aggregation contributes to the interpretation of biochemical and functional data and paves the way for new strategies in the modulation of CK2 activity and for the design of non-ATP-competitive inhibitors targeting the interaction between the α catalytic and the β regulatory subunits. PubMed: 22506723DOI: 10.1021/cb300054n PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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