Evidence map›Paper›PMID 29567833›Full record

ArticleThe Journal of biological chemistry2018

Structural basis for the ability of MBD domains to bind methyl-CG and TG sites in DNA.

Ke Liu, Chao Xu, Ming Lei, Ally Yang, Peter Loppnau, Timothy R Hughes, Jinrong Min

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Review
  3. 8-Oxoguanine: A Lesion, an Epigenetic Mark, or a Molecular Signal?International journal of molecular sciences · 2025
    Review
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  16. Article
  17. The MECP2-TRD domain interacts with the DNMT3A-ADD domain at the H3-tail binding site.Protein science : a publication of the Protein Society · 2023
    Article
  18. Review
  19. Article
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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

7 authors at 1 institution in 1 country.

Ke LiuStructural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7; Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Chao XuStructural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7; Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Ming LeiStructural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7; Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Ally YangDonnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1.
Peter LoppnauStructural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Timothy R HughesDonnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1.
Jinrong MinStructural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7; Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada. Electronic address: jr.min@utoronto.ca.
University of Toronto · CA

Funding

Wellcome Trust
6 · The paper itself

Abstract

Cytosine methylation is a well-characterized epigenetic mark and occurs at both CG and non-CG sites in DNA. Both methylated CG (mCG)- and mCH (H = A, C, or T)-containing DNAs, especially mCAC-containing DNAs, are recognized by methyl-CpG-binding protein 2 (MeCP2) to regulate gene expression in neuron development. However, the molecular mechanism involved in the binding of methyl-CpG-binding domain (MBD) of MeCP2 to these different DNA motifs is unclear. Here, we systematically characterized the DNA-binding selectivities of the MBD domains in MeCP2 and MBD1-4 with isothermal titration calorimetry-based binding assays, mutagenesis studies, and X-ray crystallography. We found that the MBD domains of MeCP2 and MBD1-4 bind mCG-containing DNAs independently of the sequence identity outside the mCG dinucleotide. Moreover, some MBD domains bound to both methylated and unmethylated CA dinucleotide-containing DNAs, with a preference for the CAC sequence motif. We also found that the MBD domains bind to mCA or nonmethylated CA DNA by recognizing the complementary TG dinucleotide, which is consistent with an overlooked ligand of MeCP2,

Indexed as

Binding SitesCalorimetryCrystallography, X-RayCytosineDNADNA-Binding ProteinsDNA MethylationEndodeoxyribonucleasesGene Expression RegulationGuanineHumansMethyl-CpG-Binding Protein 2MutagenesisNucleotidesProtein DomainsThymineCytosineDNADNA-Binding ProteinsEndodeoxyribonucleasesGuanineMBD1 protein, humanMBD2 protein, humanMBD3 protein, humanMBD4 protein, humanMECP2 protein, humanMethyl-CpG-Binding Protein 2NucleotidesThymineTranscription Factors5-methylcytosineCAC motifCpH methylationDNA methylationepigeneticsgene regulationmethyl-CpG–binding domain (MBD)methyl-CpG–binding protein 2X-ray crystallography

Identifiers

PMID29567833
PMCPMC5949999
OpenAlexW2791103809

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.