The Catalytic Subunit of Human Protein Kinase CK2 Structurally Deviates from Its Maize Homologue in Complex with the Nucleotide Competitive Inhibitor Emodin

Journal of Molecular Biology

Volumn 377, Issue 1, 2008, Pages 1-8

  Raaf, Jennifer ^a   Klopffleisch, Karsten ^a   Issinger, Olaf Georg ^b   Niefind, Karsten ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

casein kinase 2; CMGC family of eukaryotic protein kinases; emodin; protein kinase CK2; protein kinase inhibitors

Indexed keywords

ADENOSINE TRIPHOSPHATE; CASEIN KINASE II; EMODIN;

ARTICLE; BINDING SITE; COMPLEX FORMATION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HUMAN; LIGAND BINDING; MAIZE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION;

EUKARYOTA; ZEA MAYS;

EID: 39649083339     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.008     Document Type: Article

References (29)

1. Hanks S.K., and Hunter T. Protein kinases. 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9 (1995) 576-596
2. Niefind K., Guerra B., Ermakowa I., and Issinger O.-G. Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. EMBO J. 20 (2001) 5320-5331
3. Guerra B., and Issinger O.-G. Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis 20 (1999) 391-408
4. Ahmed K., Gerber D.A., and Cochet C. Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol. 12 (2002) 225-230
5. Allende J.E., and Allende C.C. Protein kinases 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J. 9 (1995) 313-323
6. Meggio F., and Pinna L.A. One-thousand-and-one substrates of protein kinase CK2?. FASEB J. 17 (2003) 349-368
7. Battistutta R., De Moliner E., Sarno S., Zanotti G., and Pinna L.A. Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole. Protein Sci. 10 (2001) 2200-2206
8. Zandomeni R., and Weinmann R. Inhibitory effect of 5,6-dichloro-1-beta-d-ribofuranosylbenzimidazole on a protein kinase. J. Biol. Chem. 259 (1984) 14804-14811
9. Moro S., Varano F., Cozza G., Pagano M.A., Zagotto G., Chilin A., et al. Pyrazoloquinazoline tricyclic system as novel scaffold to design new kinase CK2 inhibitors. Lett. Drug Des. Discovery 3 (2006) 281-284
10. Füllbeck M., Huang X., Dumdey R., Frommel C., Dubiel W., and Preissner R. Novel curcumin- and emodin-related compounds identified by in silico 2D/3D conformer screening induce apoptosis in tumor cells. BMC Cancer 5 (2005) 97
11. Battistutta R., Sarno S., De Moliner E., Papinutto E., Zanotti G., and 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 (2000) 29618-29622
12. Yim H., Lee Y.H., Lee C.H., and Lee S.K. Emodin, an anthraquinone derivative isolated from the rhizomes of Rheum palmatum, selectively inhibits the activity of casein kinase II as a competitive inhibitor. Planta Med. 65 (1999) 9-13
13. Olsen B.B., Bjørling-Poulsen M., and Guerra B. Emodin negatively affects the phosphoinositide 3-kinase/AKT signalling pathway: a study on its mechanism of action. Int. J. Biochem. Cell Biol. 39 (2007) 227-237
14. De Moliner E., Moro S., Sarno S., Zagotto G., Zanotti G., Pinna L.A., and Battistutta R. Inhibition of protein kinase CK2 by anthraquinone-related compounds. A structural insight. J. Biol. Chem. 278 (2003) 1831-1836
15. Sarno S., Ruzzene M., Frascella P., Pagano M.A., Meggio F., Zambon A., et al. Development and exploitation of CK2 inhibitors. Mol. Cell. Biochem. 274 (2005) 69-76
16. Niefind, K. (2004). 50 Jahre Proteinkinase CK2-ein Beitrag zur Strukturbiologie eukaryontischer Proteinkinasen. Habilitation thesis, University of Cologne; http://kups.ub.uni-koeln.de/volltexte/2006/1860
17. Ermakova I., Boldyreff B., Issinger O.-G., and Niefind K. Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit. J. Mol. Biol. 330 (2003) 925-934
18. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
19. Collaborative Computing Project, Number 4. CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
20. Schuettelkopf A.W., and van Aalten D.M.F. PRODRG-a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 (2004) 1355-1363
21. Jones T.A., Zou J.-Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr., Sect. A: Found. Crystallogr. 47 (1991) 110-119
22. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 (2004) 2126-2132
23. Niefind K., Yde C.W., Ermakova I., and Issinger O.-G. Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases. J. Mol. Biol. 370 (2007) 427-438
24. Schomburg D., and Reichelt J. BRAGI: a comprehensive protein modeling program system. J. Mol. Graphics 6 (1988) 161-165
25. Esnouf R.M. An extensively modified version of MolScript that include greatly enhanced coloring capabilities. J. Mol. Graphics 15 (1997) 132-134
26. Merrit E.A., and Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277 (1997) 505-524
27. Helms V., and McCammon J.A. Kinase conformations: a computational study of the effect of ligand binding. Protein Sci. 6 (1997) 2336-2343
28. Traxler P., and Furet P. Strategies toward the design of novel and selective protein tyrosine kinase inhibitors. Pharmacol. Ther. 82 (1999) 195-206
29. Battistutta R., Mazzorana M., Cendron L., Bortolato A., Sarno S., Kazimierczuk Z., et al. The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules. ChemBioChem 8 (2007) 1804-1809