Evidence map›Paper›PMID 21423167›Full record

ArticleNature2011

Crystal structure of inhibitor of κB kinase β.

Guozhou Xu, Yu-Chih Lo, Qiubai Li, Gennaro Napolitano, Xuefeng Wu, Xuliang Jiang, Michel Dreano, Michael Karin, Hao Wu

Abstract read
In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing 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

123 citing papers in PubMed.

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  16. Salvimulticanol from3 Biotech · 2024
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  17. Solidagenone fromPharmaceuticals (Basel, Switzerland) · 2024
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  18. Chronic Treatment withInternational journal of molecular sciences · 2024
    Article
  19. Computational analysis of regulatory regions in human protein kinases.Protein science : a publication of the Protein Society · 2023
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Guozhou XuDepartment of Biochemistry, Weill Cornell Medical College, New York, New York 10021, USA.
Yu-Chih Lo
Qiubai Li
Gennaro Napolitano
Xuefeng Wu
Xuliang Jiang
Michel Dreano
Michael Karin
Hao Wu

Funding

Structural Studies of Protein Caspase InhibitorsR01AI050872 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI WU, HAO · 2002 to 2012
$3.6M
Structural and functional studies of the IkappaB kinase (IKK) complexR01AI079260 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI WU, HAO · 2009 to 2013
$1.9M
NIAID NIH HHS R01 AI050872NIAID NIH HHS R01 AI079260
6 · The paper itself

Abstract

Inhibitor of κB (IκB) kinase (IKK) phosphorylates IκB proteins, leading to their degradation and the liberation of nuclear factor κB for gene transcription. Here we report the crystal structure of IKKβ in complex with an inhibitor, at a resolution of 3.6 Å. The structure reveals a trimodular architecture comprising the kinase domain, a ubiquitin-like domain (ULD) and an elongated, α-helical scaffold/dimerization domain (SDD). Unexpectedly, the predicted leucine zipper and helix-loop-helix motifs do not form these structures but are part of the SDD. The ULD and SDD mediate a critical interaction with IκBα that restricts substrate specificity, and the ULD is also required for catalytic activity. The SDD mediates IKKβ dimerization, but dimerization per se is not important for maintaining IKKβ activity and instead is required for IKKβ activation. Other IKK family members, IKKα, TBK1 and IKK-i, may have a similar trimodular architecture and function.

Indexed as

Amino Acid MotifsAnimalsBiocatalysisCrystallography, X-RayEnzyme ActivationHumansI-kappa B KinaseModels, MolecularProtein BindingProtein MultimerizationProtein Structure, TertiarySubstrate SpecificityUbiquitinXenopus laevisI-kappa B KinaseUbiquitin

Identifiers

PMID21423167
PMCPMC3081413

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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.