Evidence map›Paper›PMID 22039098›Full record

ArticleNucleic acids research2012

Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody.

Young-Jun Park, Els Pardon, Meiting Wu, Jan Steyaert, Wim G J Hol

Abstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Insights into Comparative Modeling of VInternational journal of molecular sciences · 2021
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. The Architecture of Trypanosoma brucei editosomes.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Nanobodies as Probes for Protein Dynamics in Vitro and in Cells.The Journal of biological chemistry · 2016
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  20. 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

5 authors.

Young-Jun ParkDepartment of Biochemistry, Biomolecular Structure Center, School of Medicine, University of Washington, PO Box 357742, Seattle WA 98195, USA.
Els Pardon
Meiting Wu
Jan Steyaert
Wim G J Hol

Funding

STRUCTURAL STUDY OF HEAT-LABILE ENTEROTOXINR01AI034501 · NIAID · UNIVERSITY OF WASHINGTON · PI HOL, WILHELMUS G. J. · 1993 to 2013
$5.4M
NIAID NIH HHS R01 AI34501
6 · The paper itself

Abstract

The parasite Trypanosoma brucei, the causative agent of sleeping sickness across sub-Saharan Africa, depends on a remarkable U-insertion/deletion RNA editing process in its mitochondrion. A approximately 20 S multi-protein complex, called the editosome, is an essential machinery for editing pre-mRNA molecules encoding the majority of mitochondrial proteins. Editosomes contain a common core of twelve proteins where six OB-fold interaction proteins, called A1-A6, play a crucial role. Here, we report the structure of two single-strand nucleic acid-binding OB-folds from interaction proteins A3 and A6 that surprisingly, form a heterodimer. Crystal growth required the assistance of an anti-A3 nanobody as a crystallization chaperone. Unexpectedly, this anti-A3 nanobody binds to both A3(OB) and A6, despite only ~40% amino acid sequence identity between the OB-folds of A3 and A6. The A3(OB)-A6 heterodimer buries 35% more surface area than the A6 homodimer. This is attributed mainly to the presence of a conserved Pro-rich loop in A3(OB). The implications of the A3(OB)-A6 heterodimer, and of a dimer of heterodimers observed in the crystals, for the architecture of the editosome are profound, resulting in a proposal of a 'five OB-fold center' in the core of the editosome.

Indexed as

Amino Acid SequenceCross ReactionsCrystallography, X-RayDimerizationMitochondrial ProteinsModels, MolecularMolecular Sequence DataProtein MultimerizationProtein Structure, TertiaryProtozoan ProteinsRNA-Binding ProteinsRNA EditingSingle-Chain AntibodiesMitochondrial ProteinsProtozoan ProteinsRNA-Binding ProteinsSingle-Chain Antibodies

Identifiers

PMID22039098
PMCPMC3287191

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

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.