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The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2.

Battistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA
J Biol Chem 275 29618-22 (2000)
Cited: 87 times
EuropePMC logo PMID: 10882732

Abstract

The structure of a complex between the catalytic subunit of Zea mays CK2 and the nucleotide binding site-directed inhibitor emodin (3-methyl-1,6,8-trihydroxyanthraquinone) was solved at 2.6-A resolution. Emodin enters the nucleotide binding site of the enzyme, filling a hydrophobic pocket between the N-terminal and the C-terminal lobes, in the proximity of the site occupied by the base rings of the natural co-substrates. The interactions between the inhibitor and CK2 alpha are mainly hydrophobic. Although the C-terminal domain of the enzyme is essentially identical to the ATP-bound form, the beta-sheet in the N-terminal domain is altered by the presence of emodin. The structural data presented here highlight the flexibility of the kinase domain structure and provide information for the design of selective ATP competitive inhibitors of protein kinase CK2.

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Related citations provided by authors (2)

  1. Crystal Structure of the Catalitic Subunit of Protein Kinase CK2 from Zea mays at 2.1 A Resolution. Niefind K, Guerra B, Pinna LA, Issinger OG, Schomburg D EMBO J. 17 2451-2462 (1998)
  2. GTP Plus Water Mimic ATP in the Active Site of Protein Kinase CK2. Niefind K, Putter M, Guerra B, Issinger OG, Schomburg D Nat. Struct. Biol. 6 1100-1103 (1999)

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