Evidence map›Paper›PMID 12727888›Full record

ArticleThe EMBO journal2003

Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4.

Janet E Deane, Joel P Mackay, Ann H Y Kwan, Eleanor Y M Sum, Jane E Visvader, Jacqueline M Matthews

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.6field-weighted citation impact, top 18% of its field
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

33 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. LDB1 establishes multi-enhancer networks to regulate gene expression.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Crystal structure of human LDB1 in complex with SSBP2.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Disparate binding kinetics by an intrinsically disordered domain enables temporal regulation of transcriptional complex formation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. Fusion-protein-assisted protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  13. Article
  14. Article
  15. Linkers in the structural biology of protein-protein interactions.Protein science : a publication of the Protein Society · 2013
    Review
  16. LIM-domain-only proteins in cancer.Nature reviews. Cancer · 2013
    Review
  17. Solution structure of a tethered Lmo2(LIM2) /Ldb1(LID) complex.Protein science : a publication of the Protein Society · 2012
    Article
  18. Article
  19. 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

6 authors at 1 institution in 1 country.

Janet E DeaneSchool of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia.
Joel P Mackay
Ann H Y Kwan
Eleanor Y M Sum
Jane E Visvader
Jacqueline M Matthews
University of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LMO2 and LMO4 are members of a small family of nuclear transcriptional regulators that are important for both normal development and disease processes. LMO2 is essential for hemopoiesis and angiogenesis, and inappropriate overexpression of this protein leads to T-cell leukemias. LMO4 is developmentally regulated in the mammary gland and has been implicated in breast oncogenesis. Both proteins comprise two tandemly repeated LIM domains. LMO2 and LMO4 interact with the ubiquitous nuclear adaptor protein ldb1/NLI/CLIM2, which associates with the LIM domains of LMO and LIM homeodomain proteins via its LIM interaction domain (ldb1-LID). We report the solution structures of two LMO:ldb1 complexes (PDB: 1M3V and 1J2O) and show that ldb1-LID binds to the N-terminal LIM domain (LIM1) of LMO2 and LMO4 in an extended conformation, contributing a third strand to a beta-hairpin in LIM1 domains. These findings constitute the first molecular definition of LIM-mediated protein-protein interactions and suggest a mechanism by which ldb1 can bind a variety of LIM domains that share low sequence homology.

Indexed as

Repressor ProteinsAdaptor Proteins, Signal TransducingAmino Acid SequenceCircular DichroismDNA-Binding ProteinsHomeodomain ProteinsInhibitor of Differentiation Protein 1LIM Domain ProteinsMetalloproteinsModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein ConformationSequence Homology, Amino AcidSpectrophotometry, UltravioletTranscription FactorsAdaptor Proteins, Signal TransducingDNA-Binding ProteinsHomeodomain ProteinsInhibitor of Differentiation Protein 1LIM Domain ProteinsLMO4 protein, humanMetalloproteinsRepressor ProteinsTranscription Factors

Identifiers

PMID12727888
PMCPMC156068
OpenAlexW2043937578

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.