Abstract
Protein kinase CK2 plays an essential role in the regulation of many cellular functions. The enzyme is an heterotetrameric complex formed by the association of two catalytic α/α′ subunits with two regulatory β subunits. High-resolution structure of the CK2β subunit revealed the presence of a zinc binding motif made by three-stranded antiparallel β sheets and two “knuckles” (Cys-X4-Cys and Cys-X2-Cys) contained in the invariant motif CPX3C-X22-CPXC. This zinc binding motif belongs to the sub-family of zinc ribbon domains. CK2β exist as a dimer in which the zinc ribbon motif makes many hydrophobic interactions with the zinc ribbon motif of the other monomer forming the protein-protein interface. Importantly, functional and biochemical studies have indicated that the integrity of the zinc binding motif which is pivotal in the formation of the CK2β homodimer, is also instrumental for the regulatory functions of this important protein.
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Filhol, O., Benitez, M.J., Cochet, C. (2005). A Zinc Ribbon Motif Is Essential for the Formation of Functional Tetrameric Protein Kinase CK2. In: Iuchi, S., Kuldell, N. (eds) Zinc Finger Proteins. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-27421-9_18
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DOI: https://doi.org/10.1007/0-387-27421-9_18
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-48229-8
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