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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Raaf, Jennifer Niefind, Karsten Brunstein, Elena Issinger, Olaf-Georg |
| Description | Country affiliation: Germany Author Affiliation: Raaf J ( Universität zu Köln, Department für Chemie, Institut fü r Biochemie, D-50674 Köln, Germany.) |
| Abstract | The protein kinase CK2 (former name: 'casein kinase 2') predominantly occurs as a heterotetrameric holoenzyme composed of two catalytic chains (CK2alpha) and two noncatalytic subunits (CK2beta). The CK2beta subunits form a stable dimer to which the CK2alpha monomers are attached independently. In contrast to the cyclins in the case of the cyclin-dependent kinases CK2beta is no on-switch of CK2alpha; rather the formation of the CK2 holoenzyme is accompanied with an overall change of the enzyme's profile including a modulation of the substrate specificity, an increase of the thermostability, and an allocation of docking sites for membranes and other proteins. In this study we used C-terminal deletion variants of human CK2alpha and CK2beta that were enzymologically fully competent and in particular able to form a heterotetrameric holoenzyme. With differential scanning calorimetry (DSC) we confirmed the strong thermostabilization effect of CK2alpha on CK2beta with an upshift of the CK2alpha melting temperature of more than 9 degrees . Using isothermal titration calorimetry (ITC) we measured a dissociation constant of 12.6 nM. This high affinity between CK2alpha and CK2beta is mainly caused by enthalpic rather than entropic contributions. Finally, we determined a crystal structure of the CK2beta construct to 2.8 A resolution and revealed by structural comparisons with the CK2 holoenzyme structure that the CK2beta conformation is largely conserved upon association with CK2alpha, whereas the latter undergoes significant structural adaptations of its backbone. |
| ISSN | 09618368 |
| e-ISSN | 1469896X |
| DOI | 10.1110/ps.037770.108 |
| Journal | Protein Science |
| Issue Number | 12 |
| Volume Number | 17 |
| Language | English |
| Publisher | Wiley-Blackwell (on behalf of The Protein Society) |
| Publisher Date | 2008-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Casein Kinase Ii Chemistry Metabolism Protein Subunits Calorimetry Genetics Crystallography, X-ray Dimerization Kinetics Models, Molecular Protein Binding Thermodynamics Transition Temperature X-ray Diffraction Research Support, Non-u.s. Gov't Discipline Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Biochemistry |
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