ArticleGenes & development1999
Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP.
Article in Genes & development, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.
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Who cites it
128 citing papers in PubMed, 277 citations in OpenAlex.
- Shared genetic architecture between the topology of brain white matter structural connectome and fluid intelligence.Communications biology · 2026Article
- Genome Wide Identification and Characterization ofInternational journal of genomics · 2026Article
- E2F1-3 activate Merkel cell polyomavirus early transcription and replication.bioRxiv : the preprint server for biology · 2025Article
- Family with sequence similarity 114 member A1 orchestrates immune evasion in triple-negative breast cancer.Signal transduction and targeted therapy · 2025Article
- LncRNA SLNCR phenocopies the E2F1 DNA binding site to promote melanoma progression.Cell reports · 2025Article
- Tissue factor signalling modifies the expression and regulation of G1/S checkpoint regulators: Implications during injury and prolonged inflammation.Molecular medicine reports · 2025Article
- Mutations found in cancer patients compromise DNA binding of the winged helix protein STK19.Scientific reports · 2024Article
- The ancient Z-DNA and Z-RNA specific Zα fold has evolved modern roles in immunity and transcription through the natural selection of flipons.Royal Society open science · 2024Article
- The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3.Communications biology · 2023Article
- Trim33 masks a non-transcriptional function of E2f4 in replication fork progression.Nature communications · 2023Article
- Structural and Functional Annotation of Hypothetical Proteins from the Microsporidia SpeciesInternational journal of molecular sciences · 2023Article
- E2F1/CKS2/PTEN signaling axis regulates malignant phenotypes in pediatric retinoblastoma.Cell death & disease · 2022Article
- Structure and function of MuvB complexes.Oncogene · 2022Review
- Biochemical and Structural Insights into the Winged Helix Domain of P150, the Largest Subunit of the Chromatin Assembly Factor 1.International journal of molecular sciences · 2022Article
- Abnormal methylation in theQRB discovery · 2022Article
- Ki-67 gene expression.Cell death and differentiation · 2021Article
- E2F4's cytoplasmic role in multiciliogenesis is mediated via an N-terminal domain that binds two components of the centriole replication machinery, Deup1 and SAS6.Molecular biology of the cell · 2021Article
- ELL Facilitates RNA Polymerase II-Mediated Transcription of Human Epidermal Proliferation Genes.The Journal of investigative dermatology · 2021Article
- FAM72, Glioblastoma Multiforme (GBM) and Beyond.Cancers · 2021Review
- Direct Regulation of DNA Repair by E2F and RB in Mammals and Plants: Core Function or Convergent Evolution?Cancers · 2021Review
68 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The E2F and DP protein families form heterodimeric transcription factors that play a central role in the expression of cell cycle-regulated genes. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins. The asymmetry in the extended binding site TTTc/gGCGCc/g is associated with an amino-terminal extension of E2F4, in which an arginine binds in the minor groove near the TTT stretch. This arginine is invariant among E2Fs but not present in DPs. E2F4 and DP2 interact through an extensive protein-protein interface, and structural features of this interface suggest it contributes to the preference for heterodimers over homodimers in DNA binding.
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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.