Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization.

@article{Chantalat1999CrystalSO,
  title={Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization.},
  author={Laurent Chantalat and Didier Leroy and Odile Filhol and Arsenio Nueda and Mar{\'i}a Jos{\'e} Benitez and Edmond M. Chambaz and Claude Cochet and Otto Dideberg},
  journal={The EMBO journal},
  year={1999},
  volume={18 11},
  pages={2930-40}
}
Protein kinase CK2 is a tetramer composed of two alpha catalytic subunits and two beta regulatory subunits. The structure of a C-terminal truncated form of the human beta subunit has been determined by X-ray crystallography to 1.7 A resolution. One dimer is observed in the asymmetric unit of the crystal. The most striking feature of the structure is the presence of a zinc finger mediating the dimerization. The monomer structure consists of two domains, one entirely alpha-helical and one… CONTINUE READING