ArticleJournal of molecular biology2010
Structure of the MADS-box/MEF2 domain of MEF2A bound to DNA and its implication for myocardin recruitment.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Myocyte Enhancer Factor-2A Gene Mutation and Coronary Artery Disease.Chinese medical journal · 2015Trial
- The Diverse Roles of the MEF2 Transcription Factor Family in Tumor Progression and Emerging Therapeutic Opportunities.Biomedicines · 2026Review
- Identification of diagnostic genes in rheumatoid arthritis using integrated bioinformatics, machine learning, and experimental validation.Frontiers in medicine · 2026Article
- Inhibition of myocyte-specific enhancer factor 2A (MEF2A) attenuates cardiac fibrosis and improves heart function by regulating the Snail1/RhoA/α-SMA pathway.Journal of bioenergetics and biomembranes · 2025Article
- Mapping the Interactions Among Class IIa Histone Deacetylases and Myocyte Enhancer Factor 2s.Journal of chemical information and modeling · 2025Article
- Combined Genome-Wide Association Study and Haplotype Analysis Identifies Candidate Genes Affecting Growth Traits of Inner Mongolian Cashmere Goats.Veterinary sciences · 2024Article
- Structural insights into the HDAC4-MEF2A-DNA complex and its implication in long-range transcriptional regulation.Nucleic acids research · 2024Article
- Effect of BovineGenes · 2023Article
- Pseudotime analysis reveals novel regulatory factors for multigenic onset and monogenic transition of odorant receptor expression.Scientific reports · 2022Article
- Evolutionary divergence of motifs in B-class MADS-box proteins of seed plants.Journal of biological research (Thessalonike, Greece) · 2021Article
- Involvement of myocyte enhancer factor 2c in the pathogenesis of autism spectrum disorder.Heliyon · 2021Review
- MEF2A Is the Trigger of Resveratrol Exerting Protection on Vascular Endothelial Cell.Frontiers in cardiovascular medicine · 2021Article
- Crystal Structures of Ternary Complexes of MEF2 and NKX2-5 Bound to DNA Reveal a Disease Related Protein-Protein Interaction Interface.Journal of molecular biology · 2020Article
- Landscape of DNA binding signatures of myocyte enhancer factor-2B reveals a unique interplay of base and shape readout.Nucleic acids research · 2020Article
- Structural Basis for Plant MADS Transcription Factor Oligomerization.Computational and structural biotechnology journal · 2019Review
- Recursive Motif Analyses Identify Brain Epigenetic Transcription Regulatory Modules.Computational and structural biotechnology journal · 2019Article
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- Protein interaction evolution from promiscuity to specificity with reduced flexibility in an increasingly complex network.Scientific reports · 2017Article
- DNA Shape versus Sequence Variations in the Protein Binding Process.Biophysical journal · 2016Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Myocyte enhancer factor 2 (MEF2) regulates specific gene expression in diverse developmental programs and adaptive responses. MEF2 recognizes DNA and interacts with transcription cofactors through a highly conserved N-terminal domain referred to as the MADS-box/MEF2 domain. Here we present the crystal structure of the MADS-box/MEF2 domain of MEF2A bound to DNA. In contrast to previous structural studies showing that the MEF2 domain of MEF2A is partially unstructured, the present study reveals that the MEF2 domain participates with the MADS-box in both dimerization and DNA binding as a single domain. The sequence divergence at and immediately following the C-terminal end of the MEF2 domain may allow different MEF2 dimers to recognize different DNA sequences in the flanking regions. The current structure also suggests that the ligand-binding pocket previously observed in the Cabin1-MEF2B-DNA complex and the HDAC9 (histone deacetylase 9)-MEF2B-DNA complex is not induced by cofactor binding but rather preformed by intrinsic folding. However, the structure of the ligand-binding pocket does undergo subtle but significant conformational changes upon cofactor binding. On the basis of these observations, we generated a homology model of MEF2 bound to a myocardin family protein, MASTR, that acts as a potent coactivator of MEF2-dependent gene expression. The model shows excellent shape and chemical complementarity at the binding interface and is consistent with existing mutagenesis data. The apo structure presented here can also serve as a target for virtual screening and soaking studies of small molecules that can modulate the function of MEF2 as research tools and therapeutic leads.
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