ArticleNucleic acids research2018
Phosphorylation of an intrinsically disordered region of Ets1 shifts a multi-modal interaction ensemble to an auto-inhibitory state.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- Affinity of drug candidates binding to SARS-CoV-2 PLpro assessed using a generalized-ensemble method.Scientific reports · 2026Article
- Enhanced ETS1 stability by DNAPKcs orchestrates transcriptional changes during chemoresistance in triple negative breast cancer.NPJ breast cancer · 2025Article
- Intrinsically Disordered Peptide Nanofibers from a Structured Motif Within Proteins.Angewandte Chemie (International ed. in English) · 2025Article
- A virtual system-coupled molecular dynamics simulation free from experimental knowledge on binding sites: Application to RNA-ligand binding free-energy landscape.Biophysics and physicobiology · 2025Article
- The impact of IDR phosphorylation on the RNA binding profiles of proteins.Trends in genetics : TIG · 2024Review
- Molecular Mechanisms of Functional Modulation of Transcriptional Coactivator PC4 via Phosphorylation on Its Intrinsically Disordered Region.ACS omega · 2023Article
- Non-Ewald methods for evaluating the electrostatic interactions of charge systems: similarity and difference.Biophysical reviews · 2022Review
- Some reflections on a career in science and a note of thanks to the contributors of this Special Issue.Biophysical reviews · 2022Article
- Zinc controls PML nuclear body formation through regulation of a paralog specific auto-inhibition in SUMO1.Nucleic acids research · 2022Article
- Extended ensemble simulations of a SARS-CoV-2 nsp1-5'-UTR complex.PLoS computational biology · 2022Article
- The auto-inhibition mechanism of transcription factor Ets-1 induced by phosphorylation on the intrinsically disordered region.Computational and structural biotechnology journal · 2022Article
- Microsecond molecular dynamics suggest that a non-synonymous mutation, frequently observed in patients with mild symptoms in Tokyo, alters dynamics of the SARS-CoV-2 main protease.Biophysics and physicobiology · 2021Article
- The diversity of molecular interactions involving intrinsically disordered proteins: A molecular modeling perspective.Computational and structural biotechnology journal · 2021Review
- Short Disordered Epitope of CRTAM Ig-Like V Domain as a Potential Target for Blocking Antibodies.International journal of molecular sciences · 2020Article
- The human CRY1 tail controls circadian timing by regulating its association with CLOCK:BMAL1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein.ACS omega · 2020Article
- Multifunnel Energy Landscapes for Phosphorylated Translation Repressor 4E-BP2 and Its Mutants.Journal of chemical theory and computation · 2020Article
- myPresto/omegagene 2020: a molecular dynamics simulation engine for virtual-system coupled sampling.Biophysics and physicobiology · 2020Article
- The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.The Journal of membrane biology · 2019Review
- Hydrogen bond donors and acceptors are generally depolarized in α-helices as revealed by a molecular tailoring approach.Journal of computational chemistry · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multi-modal interactions are frequently observed in intrinsically disordered regions (IDRs) of proteins upon binding to their partners. In many cases, post-translational modifications in IDRs are accompanied by coupled folding and binding. From both molecular simulations and biochemical experiments with mutational studies, we show that the IDR including a Ser rich region (SRR) of the transcription factor Ets1, just before the DNA-binding core domain, undergoes multi-modal interactions when the SRR is not phosphorylated. In the phosphorylated state, the SRR forms a few specific complex structures with the Ets1 core, covering the recognition helix in the core and drastically reducing the DNA binding affinities as the auto-inhibitory state. The binding kinetics of mutated Ets1 indicates that aromatic residues in the SRR can be substituted with other hydrophobic residues for the interactions with the Ets1 core.
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