Evidence map›Paper›PMID 16335523›Full record

ArticleMolecular and cellular biochemistry2005

Primary and secondary interactions between CK2alpha and CK2beta lead to ring-like structures in the crystals of the CK2 holoenzyme.

Karsten Niefind, Olaf-Georg Issinger

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Article in Molecular and cellular biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 43 citations in OpenAlex.

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  5. Predictive functional, statistical and structural analysis ofFrontiers in molecular biosciences · 2022
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  6. Review
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  19. Characterization of protein kinase CK2 from Trypanosoma brucei.Molecular and biochemical parasitology · 2007
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Karsten NiefindUniversität zu Köln, Institut für Biochemie, Zülpicher Strasse 47, D-50674 Köln, Germany. Karsten.Niefind@uni-koeln.de
Olaf-Georg Issinger
University of Cologne · DEUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase CK2 predominantly exists as a heterotetrameric holoenyzme consisting of two catalytic subunits (CK2alpha) and two non-catalytic subunits (CK2beta). Early investigations which we review here had revealed the presence of two types of contacts between CK2alpha and CK2beta: a primary interaction responsible for the stability of the CK2 holoenzyme and stimulatory for the catalytic activity, and a secondary interaction which is inhibitory and in which the acidic loop of CK2beta associates with the basic stretch and the (p+1)-loop of CK2alpha. At the end of the last decade both types of interactions were assumed to occur within the same tetrameric complex. The CK2 holoenyzme structure, however, suggested that the secondary interactions must happen between different CK2 tetramers. Such a behaviour should lead to higher-ordered aggregates consistent with several previous reports about a distinct aggregation propensity of CK2. We demonstrate here that in the CK2 holoenzyme crystals contacts between different CK2 tetramers exists which provide structural details of the secondary CK2alpha/CK2beta interactions. These mainly ionic interactions lead to trimeric rings of CK2 holoenzymes in the crystal. In these rings each CK2 tetramer possesses one CK2alpha subunit open for substrate binding and another one whose active site is blocked by a secondary contact with CK2beta from a neighbouring tetramer. This observation fits to previous findings that salt-sensitive ring-like aggregates of CK2 holoenzymes can exist which possess significant catalytic activity. Furthermore it suggests that earlier ideas about a regulatory role of the enzyme's aggregation propensity may be worth to be revitalised.

Indexed as

Catalytic DomainModels, MolecularBinding SitesCasein Kinase IICrystallizationDimerizationHoloenzymesProtein ConformationCasein Kinase IIHoloenzymes

Identifiers

PMID16335523
OpenAlexW2007059241

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.