Evidence map›Paper›PMID 22658747›Full record

ArticleStructure (London, England : 1993)2012

Structural insights into the role of domain flexibility in human DNA ligase IV.

Takashi Ochi, Qian Wu, Dimitri Y Chirgadze, J Günter Grossmann, Victor M Bolanos-Garcia, Tom L Blundell

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Review
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  17. Organization and dynamics of the nonhomologous end-joining machinery during DNA double-strand break repair.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. Article
  20. Review
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

6 authors.

Takashi OchiDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK. to237@cam.ac.uk
Qian Wu
Dimitri Y Chirgadze
J Günter Grossmann
Victor M Bolanos-Garcia
Tom L Blundell

Funding

Wellcome Trust
6 · The paper itself

Abstract

Knowledge of the architecture of DNA ligase IV (LigIV) and interactions with XRCC4 and XLF-Cernunnos is necessary for understanding its role in the ligation of double-strand breaks during nonhomologous end joining. Here we report the structure of a subdomain of the nucleotidyltrasferase domain of human LigIV and provide insights into the residues associated with LIG4 syndrome. We use this structural information together with the known structures of the BRCT/XRCC4 complex and those of LigIV orthologs to interpret small-angle X-ray scattering of LigIV in complex with XRCC4 and size exclusion chromatography of LigIV, XRCC4, and XLF-Cernunnos. Our results suggest that the flexibility of the catalytic region is limited in a manner that affects the formation of the LigIV/XRCC4/XLF-Cernunnos complex.

Indexed as

DNA RepairCatalytic DomainChromatography, GelDNADNA-Binding ProteinsDNA Breaks, Double-StrandedDNA Ligase ATPDNA LigasesDNA NucleotidyltransferasesDNA Repair EnzymesEscherichia coliHumansModels, MolecularProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryDNADNA-Binding ProteinsDNA Ligase ATPDNA LigasesDNA NucleotidyltransferasesDNA Repair EnzymesLIG4 protein, humanNHEJ1 protein, humanRecombinant ProteinsXRCC4 protein, human

Identifiers

PMID22658747
PMCPMC3391681

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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.