1F0Q

CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN

Summary for 1F0Q

• Entry DOI: 10.2210/pdb1f0q/pdb
• Related: 1A6O 1DAW 1DAY 1DS5
• Descriptor: PROTEIN KINASE CK2, ALPHA SUBUNIT, 3-METHYL-1,6,8-TRIHYDROXYANTHRAQUINONE (3 entities in total)
• Functional Keywords: protein kinase-inhibitor complex, transferase
• Biological source: Zea mays
• Total number of polymer chains: 1
• Total formula weight: 39561.40

Authors

Battistutta, R.,Sarno, S.,De Moliner, E.,Papinutto, E.,Zanotti, G.,Pinna, L.A. (deposition date: 2000-05-17, release date: 2001-05-23, Last modification date: 2024-02-07)

Primary citation

Battistutta, R.,Sarno, S.,De Moliner, E.,Papinutto, E.,Zanotti, G.,Pinna, L.A.
The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2.
J.Biol.Chem., 275:29618-29622, 2000

PubMed 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.

PubMed: 10882732
DOI: 10.1074/jbc.M004257200

Experimental method

X-RAY DIFFRACTION (2.63 Å)