ArticleMolecular and cellular biochemistry2001
Characterization of CK2 holoenzyme variants with regard to crystallization.
Article in Molecular and cellular biochemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- The New Role for an Old Kinase: Protein Kinase CK2 Regulates Metal Ion Transport.Pharmaceuticals (Basel, Switzerland) · 2016Review
- Identification of a novel potent, selective and cell permeable inhibitor of protein kinase CK2 from the NIH/NCI Diversity Set Library.Molecular and cellular biochemistry · 2015Article
- Functional display of heterotetrameric human protein kinase CK2 on Escherichia coli: a novel tool for drug discovery.Microbial cell factories · 2015Article
- Biochemical characterization of CK2alpha and alpha' paralogues and their derived holoenzymes: evidence for the existence of a heterotrimeric CK2alpha'-holoenzyme forming trimeric complexes.Molecular and cellular biochemistry · 2008Article
- Minimal CK2 activity required for yeast growth.Molecular and cellular biochemistry · 2005Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A search for strategies was conducted in order to obtain a human protein kinase CK2 preparation which would be suitable for crystallization, despite the fact that the recombinant enzyme is abundant and can be readily purified to homogeneity. This seemingly contradiction is based on the fact that the catalytic subunit moiety of the human CK2 holoenzyme is not stable neither as a free subunit nor in the tetrameric complex. All attempts to prevent degradation failed. Hence, alternative approaches were designed in order to avoid this degradation, which was expected to hamper any crystallization efforts severely. One of the approaches chosen was the production of a chimeric holoenzyme made up from a human regulatory subunit and a catalytic subunit from Z. mays. The plant catalytic subunit, in contrast to the human counterpart is very stable and does not undergo this kind of degradation. The second strategy to tackle the problem of instability was to produce the homologous recombinant human CK2 holoenzyme and then, instead of trying to avoid degradation, attempt to accelerate degradation until all catalytic subunit material was converted to the degraded form, i.e. a 40 kDa polypeptide.
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Registered trials
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