ArticlePLoS computational biology2013
On the importance of polar interactions for complexes containing intrinsically disordered proteins.
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 40 papers.
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40 citing papers in PubMed.
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- AlphaFold-Multimer accurately captures interactions and dynamics of intrinsically disordered protein regions.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Autoinhibited Protein Database: a curated database of autoinhibitory domains and their autoinhibition mechanisms.Database : the journal of biological databases and curation · 2024Article
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- Electronic Polarization at the Interface between the p53 Transactivation Domain and Two Binding Partners.The journal of physical chemistry. B · 2022Article
- A unified statistical potential reveals that amino acid stickiness governs nonspecific recruitment of client proteins into condensates.Protein science : a publication of the Protein Society · 2022Article
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- A quantitative calcium phosphate nanocluster model of the casein micelle: the average size, size distribution and surface properties.European biophysics journal : EBJ · 2021Article
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- Protein-Protein Interactions Mediated by Intrinsically Disordered Protein Regions Are Enriched in Missense Mutations.Biomolecules · 2020Article
- Dissecting the Energetics of Intrinsically Disordered Proteins via a Hybrid Experimental and Computational Approach.The journal of physical chemistry. B · 2019Article
- Protein Abundance Biases the Amino Acid Composition of Disordered Regions to Minimize Non-functional Interactions.Journal of molecular biology · 2019Article
- Analysis of Heterodimeric "Mutual Synergistic Folding"-Complexes.International journal of molecular sciences · 2019Article
- RNA structure drives interaction with proteins.Nature communications · 2019Article
- Designed Mutations Alter the Binding Pathways of an Intrinsically Disordered Protein.Scientific reports · 2019Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
There is a growing recognition for the importance of proteins with large intrinsically disordered (ID) segments in cell signaling and regulation. ID segments in these proteins often harbor regions that mediate molecular recognition. Coupled folding and binding of the recognition regions has been proposed to confer high specificity to interactions involving ID segments. However, researchers recently questioned the origin of the interaction specificity of ID proteins because of the overrepresentation of hydrophobic residues in their interaction interfaces. Here, we focused on the role of polar and charged residues in interactions mediated by ID segments. Making use of the extended nature of most ID segments when in complex with globular proteins, we first identified large numbers of complexes between globular proteins and ID segments by using radius-of-gyration-based selection criteria. Consistent with previous studies, we found the interfaces of these complexes to be enriched in hydrophobic residues, and that these residues contribute significantly to the stability of the interaction interface. However, our analyses also show that polar interactions play a larger role in these complexes than in structured protein complexes. Computational alanine scanning and salt-bridge analysis indicate that interfaces in ID complexes are highly complementary with respect to electrostatics, more so than interfaces of globular proteins. Follow-up calculations of the electrostatic contributions to the free energy of binding uncovered significantly stronger Coulombic interactions in complexes harbouring ID segments than in structured protein complexes. However, they are counter-balanced by even higher polar-desolvation penalties. We propose that polar interactions are a key contributing factor to the observed high specificity of ID segment-mediated interactions.
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