Evidence map›Paper›PMID 38960718›Full record

ArticleGenes & development2024

Structural and biochemical analyses of the nuclear IκBζ protein in complex with the NF-κB p50 homodimer.

Norman Zhu, W Eric Rogers, David K Heidary, Tom Huxford

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Article in Genes & development, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. 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

4 authors.

Norman ZhuStructural Biochemistry Laboratory, Department of Chemistry and Biochemistry, San Diego State University, San Diego, California 92182, USA.
W Eric RogersStructural Biochemistry Laboratory, Department of Chemistry and Biochemistry, San Diego State University, San Diego, California 92182, USA.
David K HeidaryDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina 27607, USA.
Tom HuxfordStructural Biochemistry Laboratory, Department of Chemistry and Biochemistry, San Diego State University, San Diego, California 92182, USA; thuxford@sdsu.edu.ORCID 0000-0002-1939-7373

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As part of the efforts to understand nuclear IκB function in NF-κB-dependent gene expression, we report an X-ray crystal structure of the IκBζ ankyrin repeat domain in complex with the dimerization domain of the NF-κB p50 homodimer. IκBζ possesses an N-terminal α helix that conveys domain folding stability. Affinity and specificity of the complex depend on a small portion of p50 at the nuclear localization signal. The model suggests that only one p50 subunit supports binding with IκBζ, and biochemical experiments confirm that IκBζ associates with DNA-bound NF-κB p50:RelA heterodimers. Comparisons of IκBζ:p50 and p50:κB DNA complex crystallographic models indicate that structural rearrangement is necessary for ternary complex formation of IκBζ and p50 with DNA.

Indexed as

Models, MolecularNF-kappa B p50 SubunitProtein BindingProtein MultimerizationAdaptor Proteins, Signal TransducingAmino Acid SequenceCell NucleusCrystallography, X-RayDNAHumansI-kappa B ProteinsTranscription Factor RelAAdaptor Proteins, Signal TransducingDNAI-kappa B ProteinsNF-kappa B p50 SubunitNFKB1 protein, humanNFKBIZ protein, humanTranscription Factor RelAIκBζNF-κBprotein structuretranscription regulationX-ray crystallography

Identifiers

PMID38960718
PMCPMC11293385

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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.