Evidence map›Paper›PMID 24130829›Full record

ArticlePloS one2013

Solution NMR structure and histone binding of the PHD domain of human MLL5.

Alexander Lemak, Adelinda Yee, Hong Wu, Damian Yap, Hong Zeng, Ludmila Dombrovski, Scott Houliston, Samuel Aparicio, Cheryl H Arrowsmith

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. CanPharmaceuticals (Basel, Switzerland) · 2024
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. MLL5 (KMT2E): structure, function, and clinical relevance.Cellular and molecular life sciences : CMLS · 2017
    Review
  14. Article
  15. G3 (Bethesda, Md.) · 2017
    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

9 authors at 4 institutions in 1 country.

Alexander LemakNortheast Structural Genomics Consortium and Ontario Cancer Institute, University Health Network, Toronto, Ontario, Canada.
Adelinda Yee
Hong Wu
Damian Yap
Hong Zeng
Ludmila Dombrovski
Scott Houliston
Samuel Aparicio
Cheryl H Arrowsmith
Structural Genomics Consortium · CABC Cancer Agency · CAUniversity of Toronto · CAUniversity Health Network · CA

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ROST, BURKHARD · 2010 to 2014
$36.9M
CIHRNIGMS NIH HHS U54 GM094597Wellcome TrustWellcome Trust 092809/Z/10/Z
6 · The paper itself

Abstract

Mixed Lineage Leukemia 5 (MLL5) is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. In addition to its catalytic domain, MLL5 contains a PHD finger domain, a protein module that is often involved in binding to the N-terminus of histone H3. Here we report the NMR solution structure of the MLL5 PHD domain showing a variant of the canonical PHD fold that combines conserved H3 binding features from several classes of other PHD domains (including an aromatic cage) along with a novel C-terminal α-helix, not previously seen. We further demonstrate that the PHD domain binds with similar affinity to histone H3 tail peptides di- and tri-methylated at lysine 4 (H3K4me2 and H3K4me3), the former being the putative product of the MLL5 catalytic reaction. This work establishes the PHD domain of MLL5 as a bone fide 'reader' domain of H3K4 methyl marks suggesting that it may guide the spreading or further methylation of this site on chromatin.

Indexed as

Catalytic DomainNuclear Magnetic Resonance, BiomolecularAmino Acid SequenceAnimalsDNA-Binding ProteinsDNA MethylationHistonesHumansModels, MolecularMolecular Sequence DataProtein BindingSolutionsDNA-Binding ProteinsHistonesKMT2E protein, humanSolutions

Identifiers

PMID24130829
PMCPMC3793974
OpenAlexW2048387831

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.