Evidence map›Paper›PMID 10357806›Full record

ArticleThe EMBO journal1999

Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization.

L Chantalat, D Leroy, O Filhol, A Nueda, M J Benitez, E M Chambaz, C Cochet, O Dideberg

Abstract read
In one paragraph

Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
–field-weighted citation impact
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

62 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The Catalytic Subunit ofInternational journal of molecular sciences · 2022
    Article
  9. Host and Viral Zinc-Finger Proteins in COVID-19.International journal of molecular sciences · 2022
    Review
  10. Review
  11. Predictive functional, statistical and structural analysis ofFrontiers in molecular biosciences · 2022
    Article
  12. Review
  13. Heliyon · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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

8 authors.

L ChantalatLaboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS/CEA, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
D Leroy
O Filhol
A Nueda
M J Benitez
E M Chambaz
C Cochet
O Dideberg

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase CK2 is a tetramer composed of two alpha catalytic subunits and two beta regulatory subunits. The structure of a C-terminal truncated form of the human beta subunit has been determined by X-ray crystallography to 1.7 A resolution. One dimer is observed in the asymmetric unit of the crystal. The most striking feature of the structure is the presence of a zinc finger mediating the dimerization. The monomer structure consists of two domains, one entirely alpha-helical and one including the zinc finger. The dimer has a crescent shape holding a highly acidic region at both ends. We propose that this acidic region is involved in the interactions with the polyamines and/or catalytic subunits. Interestingly, conserved amino acid residues among beta subunit sequences are clustered along one linear ridge that wraps around the entire dimer. This feature suggests that protein partners may interact with the dimer through a stretch of residues in an extended conformation.

Indexed as

Amino Acid SequenceBinding SitesCasein Kinase IIConserved SequenceCrystallizationCrystallography, X-RayDimerizationHumansHydrogen BondingModels, MolecularMolecular Sequence DataPeptide FragmentsProtein BindingProtein ConformationProtein FoldingProtein Serine-Threonine KinasesCasein Kinase IIPeptide FragmentsProtein Serine-Threonine KinasesSpermineZinc

Identifiers

PMID10357806
PMCPMC1171375

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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.