The interaction of CK2α and CK2β, the subunits of protein kinase CK2, requires CK2β in a preformed conformation and is enthalpically driven

Protein Science

Volumn 17, Issue 12, 2008, Pages 2180-2186

  Raaf, Jennifer ^a   Brunstein, Elena ^a   Issinger, Olaf Georg ^b   Niefind, Karsten ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

Casein kinase 2; Catalytic subunit CK2 ; Isothermal titration and differential scanning calorimetry; Protein kinase CK2; Regulatory subunit CK2 ; Thermostabilization of CK2 by CK2 ; X ray crystallography

Indexed keywords

CASEIN KINASE II; CASEIN KINASE II ALPHA; CASEIN KINASE II BETA; CYCLINE; HOLOENZYME; MONOMER; UNCLASSIFIED DRUG; PROTEIN SUBUNIT;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; ENZYME CONFORMATION; INFORMATION PROCESSING; ISOTHERMAL TITRATION CALORIMETRY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; THERMODYNAMICS; THERMOSTABILITY; CALORIMETRY; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; GENETICS; HUMAN; KINETICS; METABOLISM; PROTEIN BINDING; TRANSITION TEMPERATURE; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

CALORIMETRY; CASEIN KINASE II; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HUMANS; KINETICS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN SUBUNITS; THERMODYNAMICS; TRANSITION TEMPERATURE; X-RAY DIFFRACTION;

EID: 56749157696     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.037770.108     Document Type: Article

References (29)

1. WAF1 peptide demonstrates flexibility of the acidic loop. Acta Crystallogr. D60: 1698-1704.
2. Bibby, A.C. and Litchfield, D.W. 2005. The multiple personalities of the regulatory subunit of protein kinase CK2: CK2-dependent and CK2-independent roles reveal a secret identity for CK2β. Int. J. Biol. Sci. 1: 67-79.
3. Bolanos-Garcia, V.M., Fernandez-Recio, J., Allende, J.E., and Blundell, T.L. 2006. Identifying interaction motifs in CK2β - a ubiquitous kinase regulatory subunit. Trends Biochem. Sci. 31: 654-661.
4. Boldyreff, B., Meggio, F., Pinna, L.A., and Issinger, O.-G. 1993. Reconstitution of normal and hyperactivated forms of casein kinase-2 by variably mutated β-subunits. Biochemistry 32: 12672-12677.
5. Buchou, T., Vernet, M., Blond, O., Jensen, H.H., Pointu, H., Olsen, B.B., Cochet, C., Issinger, O.-G., and Boldyreff, B. 2003. Disruption of the regulatory β subunit of protein kinase CK2 in mice leads to a cell-autonomous defect and early embryonic lethality. Mol. Cell. Biol. 23: 908-915.
6. Chantalat, L., Leroy, D., Filhol, O., Nueda, A., Benitez, M.J., Chambaz, E.M., Cochet, C., and Dideberg, O. 1999a. Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization. EMBO J. 18: 2930-2940.
7. Chantalat, L., Leroy, D., Filhol, O., Quitaine, N., Chambaz, E.M., Cochet, C., and Dideberg, O. 1999b. Crystallization and preliminary X-ray diffraction analysis of the regulatory subunit of human protein kinase CK2. Acta Crystallogr. D Biol. Crystallogr. 55: 895-897.
8. Collaborative Computational Project, Number 4. 1994. CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50: 760-763.
9. Dobrowolska, G., Meggio, F., Szczegielniak, J., Muszynska, G., and Pinna, L.A. 1992. Purification and characterization of maize seedling casein kinase IIB, a monomeric enzyme immunologically related to the a subunit of animal casein kinase-2. Eur. J. Biochem. 204: 299-303.
10. Ermakova, I., Boldyreff, B., Issinger, O.-G., and Niefind, K. 2003. Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit. J. Mol. Biol. 330: 925-934.
11. Esnouf, R.M. 1997. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15: 132-134.
12. Issinger, O.-G., Brockel, C., Boldyreff, B., and Pelton, J.T. 1992. Characterization of the α and β subunits of casein kinase 2 by far-UV CD spectroscopy. Biochemistry 31: 6098-6103.
13. Jones, S. and Thornton, J.M. 1996. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. 93: 13-20.
14. Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. 1991. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr. A 47: 110-119.
15. Laudet, B., Barette, C., Dulery, V., Renaudet, O., Dumy, P., Metz, A., Prudent, R., Deshiere, A., Dideberg, O., Filhol, O., et al. 2007. Structure-based design of small peptide inhibitors of protein kinase CK2 subunit interaction. Biochem. J. 408: 363-373.
16. Lensink, M.F., Méndez, R., and Wodak, S.J. 2007. Docking and scoring protein complexes: CAPRI 3rd edition. Proteins 69: 704-718.
17. Martel, V., Filhol, O., Nueda, A., and Cochet, C. 2002. Dynamic localization/association of protein kinase CK2 subunits in living cells: A role in its cellular regulation? Ann. N. Y. Acad. Sci. 973: 272-277.
18. Merrit, E.A. and Bacon, D.J. 1997. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277: 505-524.
19. Niefind, K., Guerra, B., Pinna, L.A., Issinger, O.-G., and Schomburg, D. 1998. Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 Å resolution. EMBO J. 17: 2451-2462.
20. Niefind, K., Guerra, B., Ermakowa, I., and Issinger, O.-G. 2001. Crystal structure of human protein kinase CK2: Insights into basic properties of the CK2 holoenzyme. EMBO J. 20: 5320-5331.
21. Niefind, K., Yde, C.W., Ermakova, I., and Issinger, O.-G. 2007. Evolved to be active: Sulfate ions define substrate recognition sites of CK2α and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases. J. Mol. Biol. 370: 427-438.
22. Nooren, I.M.A. and Thornton, J.M. 2003. Structural characterization and functional significance of transient protein-protein interactions. J. Mol. Biol. 325: 991-1018.
23. Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
24. Pinna, L.A. 2003. The raison d'être of constitutively active protein kinases: The lesson of CK2. Acc. Chem. Res. 36: 378-384.
25. Raaf, J., Brunstein, E., Issinger, O.-G., and Niefind, K. 2008. The subunit interface of protein kinase CK2 harbors a small molecule binding pocket. Chem. Biol. 15: 111-117.
26. Rodriguez, F.A., Contreras, C., Bolanos-Garcia, V., and Allende, J.E. 2008. Protein kinase CK2 as an ectokinase: The role of the regulatory CK2β subunit. Proc. Natl. Acad. Sci. 105: 5693-5698.
27. Sarrouilhe, D., Filhol, O., Leroy, D., Bonello, G., Baudry, M., Chambaz, E.M., and Cochet, C. 1998. The tight association of protein kinase CK2 with plasma membranes is mediated by a specific domain of its regulatory β-subunit. Biochim. Biophys. Acta 1403: 199-210.
28. Schomburg, D. and Reichelt, J. 1988. BRAGI: A comprehensive protein modeling program system. J. Mol. Graph. 6: 161-165.
29. Wells, J.A. and McClendon, C.L. 2007. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450: 1001-1009.