Evidence map›Paper›PMID 22849347›Full record

ArticleBiochemistry2012

Crystal structure of the human NKX2.5 homeodomain in complex with DNA target.

Lagnajeet Pradhan, Caroli Genis, Peyton Scone, Ellen O Weinberg, Hideko Kasahara, Hyun-Joo Nam

Abstract read
In one paragraph

Article in Biochemistry, 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
2.1field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Crystal structure of the NKX2-1 homeodomain bound to a palindromic DNA recognition sequence.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. Article
  3. Article
  4. A Novel Missense Heterozygous Mutation inJournal of pediatric genetics · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Disease-associated non-coding variants alter NKX2-5 DNA-binding affinity.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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 3 institutions in 1 country.

Lagnajeet PradhanDepartment of Bioengineering, University of Texas at Dallas, Richardson, TX 75080, USA.
Caroli Genis
Peyton Scone
Ellen O Weinberg
Hideko Kasahara
Hyun-Joo Nam
University of Florida · USThe University of Texas at Dallas · USBoston University · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
Nkx2.5-dependent pathways in postnatal cardiomyocytesR01HL081577 · NHLBI · UNIVERSITY OF FLORIDA · PI KASAHARA, HIDEKO · 2005 to 2009
$1.9M
NCRR NIH HHS P41 RR001646NCRR NIH HHS RR-01646NHLBI NIH HHS HL081577NHLBI NIH HHS R01 HL081577NIGMS NIH HHS DMR-0225180
6 · The paper itself

Abstract

NKX2.5 is a homeodomain containing transcription factor regulating cardiac formation and function, and its mutations are linked to congenital heart disease. Here we provide the first report of the crystal structure of the NKX2.5 homeodomain in complex with double-stranded DNA of its endogenous target, locating within the proximal promoter -242 site of the atrial natriuretic factor gene. The crystal structure, determined at 1.8 Å resolution, demonstrates that NKX2.5 homeodomains occupy both DNA binding sites separated by five nucleotides without physical interaction between themselves. The two homeodomains show identical conformation despite the differences in the DNA sequences they bind, and no significant bending of the DNA was observed. Tyr54, absolutely conserved in NK2 family proteins, mediates sequence-specific interaction with the TAAG motif. This high resolution crystal structure of NKX2.5 protein provides a detailed picture of protein and DNA interactions, which allows us to predict DNA binding of mutants identified in human patients.

Indexed as

Amino Acid SequenceAtrial Natriuretic FactorCrystallography, X-RayDNAHeart Defects, CongenitalHomeobox Protein Nkx-2.5Homeodomain ProteinsHumansModels, MolecularMolecular Sequence DataMutation, MissensePromoter Regions, GeneticProtein ConformationThermodynamicsTranscription FactorsAtrial Natriuretic FactorDNAHomeobox Protein Nkx-2.5Homeodomain ProteinsNKX2-5 protein, humanTranscription Factors

Identifiers

PMID22849347
PMCPMC3448007
OpenAlexW2056656436

What OpenQuestion holds

Textmetadata
LicenceTDM
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.