ArticleJournal of the American Chemical Society2020
More Than π-π-π Stacking: Contribution of Amide-π and CH-π Interactions to Crotonyllysine Binding by the AF9 YEATS Domain.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Eyes Toward the Clinic: Selective Inhibition and Degradation Approaches to Bromodomain-Containing Proteins.Chembiochem : a European journal of chemical biology · 2026Review
- Sol-gel interconvertible 62-component dodecahedra assembled via amide-π-assisted anion-coordination nanoarchitectonics.Science advances · 2026Article
- Chromatin Regulatory Targets for Anticancer Therapeutics.Chemical reviews · 2025Review
- Development of Chemical Tools for the Human YEATS Domain.ACS chemical biology · 2025Review
- The Transcription Machinery and the Driving Force of the Transcriptional Molecular Condensate: The Role of Phosphates.Current issues in molecular biology · 2025Article
- Negative Cooperativity in the UHRF1 TTD-PHD Dual Domain Masks the Contributions of Cation-π Interactions between Trimethyllysine and the TTD Aromatic Cage.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Hyperthermophilic xylanase and thermophilicity analysis by molecular dynamic simulation with quantum mechanics.Applied microbiology and biotechnology · 2024Article
- Article
- WDR5 Binding to Histone Serotonylation Is Driven by an Edge-Face Aromatic Interaction with Unexpected Electrostatic Effects.Journal of the American Chemical Society · 2024Article
- Contribution of Electrostatic CHJournal of the American Chemical Society · 2024Article
- Leveraging a Phage-Encoded Noncanonical Amino Acid: A Novel Pathway to Potent and Selective Epigenetic Reader Protein Inhibitors.ACS central science · 2024Article
- Trimethyllysine Reader Proteins Exhibit Widespread Charge-Agnostic Binding via Different Mechanisms to Cationic and Neutral Ligands.Journal of the American Chemical Society · 2024Article
- Inadequate structural constraint on Fab approach rather than paratope elicitation limits HIV-1 MPER vaccine utility.Nature communications · 2023Article
- Identification of multidentate tyrosyl-DNA phosphodiesterase 1 (TDP1) inhibitors that simultaneously access the DNA, protein and catalytic-binding sites by oxime diversification.RSC chemical biology · 2023Article
- Molecular Recognition of Methacryllysine and Crotonyllysine by the AF9 YEATS Domain.International journal of molecular sciences · 2023Article
- Revealing the Molecular Interactions between Human ACE2 and the Receptor Binding Domain of the SARS-CoV-2 Wild-Type, Alpha and Delta Variants.International journal of molecular sciences · 2023Article
- Evaluation of acyllysine isostere interactions with the aromatic pocket of the AF9 YEATS domain.Protein science : a publication of the Protein Society · 2023Article
- The Role of Tryptophan in π Interactions in Proteins: An Experimental Approach.Journal of the American Chemical Society · 2022Article
- A Conformationally Stable Acyclic β-Hairpin Scaffold Tolerating the Incorporation of Poorly β-Sheet-Prone Amino Acids.Chembiochem : a European journal of chemical biology · 2022Article
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Authors and funding
6 authors.
Funding
Abstract
Lysine crotonylation (Kcr) is a histone post-translational modification that is implicated in numerous epigenetic pathways and diseases. Recognition of Kcr by YEATS domains has been proposed to occur through intermolecular amide-π and alkene-π interactions, but little is known about the driving force of these key interactions. Herein, we probed the recognition of lysine crotonylation and acetylation by the AF9 YEATS domain through incorporation of noncanonical Phe analogs with distinct electrostatics at two positions. We found that amide-π interactions between AF9 and acyllysines are electrostatically tunable, with electron-rich rings providing more favorable interactions. This differs from trends in amide-heteroarene interactions and provides insightful information for therapeutic design. Additionally, we report for the first time that CH-π interactions at Phe28 directly contribute to AF9's recognition of acyllysines, illuminating differences among YEATS domains, as this residue is not highly conserved but has been shown to impart selectivity for specific post-translational modification.
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