ArticlePLoS computational biology2013
Polycation-π interactions are a driving force for molecular recognition by an intrinsically disordered oncoprotein family.
Article in PLoS computational biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 69 citations in OpenAlex.
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- Barrier properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length.Nature communications · 2023Article
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- Minimalist Design of an Intrinsically Disordered Protein-Mimicking Scaffold for an Artificial Membraneless Organelle.ACS central science · 2022Article
- Atomic resolution dynamics of cohesive interactions in phase-separated Nup98 FG domains.Nature communications · 2022Article
- Physics-driven coarse-grained model for biomolecular phase separation with near-quantitative accuracy.Nature computational science · 2021Article
- Matrin3: Disorder and ALS Pathogenesis.Frontiers in molecular biosciences · 2021Review
- Molecular Details of Protein Condensates Probed by Microsecond Long Atomistic Simulations.The journal of physical chemistry. B · 2020Article
- Comparative roles of charge,Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Identifying sequence perturbations to an intrinsically disordered protein that determine its phase-separation behavior.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Implications of kappa-casein evolutionary diversity for the self-assembly and aggregation of casein micelles.Royal Society open science · 2019Article
- Intrinsically Disordered Linkers Impart Processivity on Enzymes by Spatial Confinement of Binding Domains.International journal of molecular sciences · 2019Article
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Authors and funding
5 authors at 3 institutions in 4 countries.
Funding
Abstract
Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions. However, some IDPs remain disordered in the bound state, a phenomenon coined "fuzziness", often characterized by IDP polyvalency, sequence-insensitivity and a dynamic ensemble of disordered bound-state conformations. Besides the above general features, specific biophysical models for fuzzy interactions are mostly lacking. The transcriptional activation domain of the Ewing's Sarcoma oncoprotein family (EAD) is an IDP that exhibits many features of fuzziness, with multiple EAD aromatic side chains driving molecular recognition. Considering the prevalent role of cation-π interactions at various protein-protein interfaces, we hypothesized that EAD-target binding involves polycation- π contacts between a disordered EAD and basic residues on the target. Herein we evaluated the polycation-π hypothesis via functional and theoretical interrogation of EAD variants. The experimental effects of a range of EAD sequence variations, including aromatic number, aromatic density and charge perturbations, all support the cation-π model. Moreover, the activity trends observed are well captured by a coarse-grained EAD chain model and a corresponding analytical model based on interaction between EAD aromatics and surface cations of a generic globular target. EAD-target binding, in the context of pathological Ewing's Sarcoma oncoproteins, is thus seen to be driven by a balance between EAD conformational entropy and favorable EAD-target cation-π contacts. Such a highly versatile mode of molecular recognition offers a general conceptual framework for promiscuous target recognition by polyvalent IDPs.
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