Structural highlights
Function
CSK2A_MAIZE Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.
Publication Abstract from PubMed
Screening for protein kinase CK2 inhibitors of the structural diversity compound library (DTP NCI/NIH) led to the discovery of 4-[(E)-(fluoren-9-ylidenehydrazinylidene)-methyl]benzoic acid (E9). E9 induces apoptotic cell death in various cancer cell lines and upon hypoxia, the compound suppresses CK2-catalyzed HSP90/Cdc37 phosphorylation and induces HIF-1alpha degradation. Furthermore, E9 exerts a strong anti-tumour activity by inducing necrosis in murine xenograft models underlining its potential to be used for cancer treatment in future clinical studies. Crystal structure analysis of human and maize CK2alpha in complex with E9 reveals unique binding properties of the inhibitor to the enzyme, accounting for its affinity and selectivity.
Protein kinase CK2 inhibition is associated with the destabilization of HIF-1alpha in human cancer cells.,Guerra B, Rasmussen TD, Schnitzler A, Jensen HH, Boldyreff BS, Miyata Y, Marcussen N, Niefind K, Issinger OG Cancer Lett. 2015 Jan 28;356(2 Pt B):751-61. doi: 10.1016/j.canlet.2014.10.026., Epub 2014 Oct 28. PMID:25449433[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Guerra B, Rasmussen TD, Schnitzler A, Jensen HH, Boldyreff BS, Miyata Y, Marcussen N, Niefind K, Issinger OG. Protein kinase CK2 inhibition is associated with the destabilization of HIF-1alpha in human cancer cells. Cancer Lett. 2015 Jan 28;356(2 Pt B):751-61. doi: 10.1016/j.canlet.2014.10.026., Epub 2014 Oct 28. PMID:25449433 doi:http://dx.doi.org/10.1016/j.canlet.2014.10.026
