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. 1998 May 1;17(9):2451–2462. doi: 10.1093/emboj/17.9.2451

Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.

K Niefind 1, B Guerra 1, L A Pinna 1, O G Issinger 1, D Schomburg 1
PMCID: PMC1170587  PMID: 9564028

Abstract

CK2alpha is the catalytic subunit of protein kinase CK2, an acidophilic and constitutively active eukaryotic Ser/Thr kinase involved in cell proliferation. A crystal structure, at 2.1 A resolution, of recombinant maize CK2alpha (rmCK2alpha) in the presence of ATP and Mg2+, shows the enzyme in an active conformation stabilized by interactions of the N-terminal region with the activation segment and with a cluster of basic residues known as the substrate recognition site. The close interaction between the N-terminal region and the activation segment is unique among known protein kinase structures and probably contributes to the constitutively active nature of CK2. The active centre is occupied by a partially disordered ATP molecule with the adenine base attached to a novel binding site of low specificity. This finding explains the observation that CK2, unlike other protein kinases, can use both ATP and GTP as phosphorylating agents.

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Selected References

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