ArticleNucleic acids research2017
Structural characterization of interactions between transactivation domain 1 of the p65 subunit of NF-κB and transcription regulatory factors.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 59 citations in OpenAlex.
- Article
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- Conformational dynamics of fuzzy interfaces in disordered protein complexes: mapping key residues and binding modes beyond NMR models.Frontiers in bioinformatics · 2026Article
- Calhm6 Governs Macrophage Polarization Through Chp1-Camk4-Creb1 Axis and Ectosomal Delivery in Inflammatory Responses.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The long non-coding RNA GAS5 contributes to the suppression of inflammatory responses by inhibiting NF-κB activity.Frontiers in pharmacology · 2024Article
- 15-keto-PGEiScience · 2023Article
- DNA-dependent protein kinase catalytic subunit binds to the transactivation domain 1 of NF-κB p65.Biochemistry and biophysics reports · 2023Article
- Structural polymorphism of the PH domain in TFIIH.Bioscience reports · 2023Article
- Article
- Network pharmacology-based exploration identified the antiviral efficacy of Quercetin isolated from mulberry leaves against enterovirus 71 via the NF-κB signaling pathway.Frontiers in pharmacology · 2023Article
- Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones.Biophysical reviews · 2022Review
- Article
- Protection against ulcerative colitis and colorectal cancer by evodiamine via anti‑inflammatory effects.Molecular medicine reports · 2022Article
- Directed mutational scanning reveals a balance between acidic and hydrophobic residues in strong human activation domains.Cell systems · 2022Article
- Hempseed (Journal of agricultural and food chemistry · 2022Article
- Molecular mimicry of NF-κB by vaccinia virus protein enables selective inhibition of antiviral responses.Nature microbiology · 2022Article
- A Dual-Site Inhibitor of CBP/p300 KIX is a Selective and Effective Modulator of Myb.Journal of the American Chemical Society · 2021Article
- Quantitative control of noise in mammalian gene expression by dynamic histone regulation.eLife · 2021Article
- COMMD10 inhibits tumor progression and induces apoptosis by blocking NF-κB signal and values up BCLC staging in predicting overall survival in hepatocellular carcinoma.Clinical and translational medicine · 2021Article
- TIMELESS inhibits breast cancer cell invasion and metastasis by down-regulating the expression of MMP9.Cancer cell international · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p65 is a member of the NF-κB family of transcriptional regulatory proteins that functions as the activating component of the p65-p50 heterodimer. Through its acidic transactivation domain (TAD), p65 has the capacity to form interactions with several different transcriptional regulatory proteins, including TFIIB, TFIIH, CREB-binding protein (CBP)/p300 and TAFII31. Like other acidic TADs, the p65 TAD contains two subdomains (p65TA1 and p65TA2) that interact with different regulatory factors depending on the target gene. Despite its role in controlling numerous NF-κB target genes, there are no high-resolution structures of p65TA1 bound to a target transcriptional regulatory factor. In this work, we characterize the interaction of p65TA1 with two factors, the Tfb1/p62 subunit of TFIIH and the KIX domain of CBP. In these complexes, p65TA1 transitions into a helical conformation that includes its characteristic ΦXXΦΦ motif (Φ = hydrophobic amino acid). Structural and functional studies demonstrate that the two binding interfaces are primarily stabilized by three hydrophobic amino acids within the ΦXXΦΦ motif and these residues are also crucial to its ability to activate transcription. Taken together, the results provide an atomic level description of how p65TA1 is able to bind different transcriptional regulatory factors needed to activate NF-κB target genes.
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