ArticleBiophysical journal2014
Evolution of specificity in protein-protein interactions.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Protein Stability, Turnover Kinetics, and Abundance Constrain the Scaling of Protein Interaction Networks.bioRxiv : the preprint server for biology · 2026Article
- Conserved interfaces mediate multiple protein-protein interactions in a prokaryotic metabolon.Molecular systems biology · 2025Article
- Towards a Holistic Understanding of the Interactions of Redox-Active Proteins.Antioxidants (Basel, Switzerland) · 2024Article
- Following the Evolutionary Paths of Dscam1 Proteins toward Highly Specific Homophilic Interactions.Molecular biology and evolution · 2024Article
- Prediction of the most deleterious non-synonymous SNPs in the human IL1B gene: evidence from bioinformatics analyses.BMC genomic data · 2024Article
- The role of promiscuous molecular recognition in the evolution of RNase-based self-incompatibility in plants.Nature communications · 2024Article
- Article
- Fever as an evolutionary agent to select immune complexes interfaces.Immunogenetics · 2022Article
- Protein Engineering in the Design of Protein-Protein Interactions: SARS-CoV-2 Inhibitors as a Test Case.Biochemistry · 2021Article
- Comprehensive Characterization of the Coding and Non-Coding Single Nucleotide Polymorphisms in the Tumor Protein p63 (TP63) Gene Using In Silico Tools.Biomolecules · 2021Article
- Pathogenic nsSNPs that increase the risks of cancers among the Orang Asli and Malays.Scientific reports · 2021Article
- Prediction of Deleterious Non-synonymous SNPs of Human STK11 Gene by Combining Algorithms, Molecular Docking, and Molecular Dynamics Simulation.Scientific reports · 2019Article
- SCRIBER: accurate and partner type-specific prediction of protein-binding residues from proteins sequences.Bioinformatics (Oxford, England) · 2019Article
- Conservation of Specificity in Two Low-Specificity Proteins.Biochemistry · 2018Article
- Monod-Wyman-Changeux Analysis of Ligand-Gated Ion Channel Mutants.The journal of physical chemistry. B · 2017Article
- The thermostability and specificity of ancient proteins.Current opinion in structural biology · 2016Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hub proteins are proteins that maintain promiscuous molecular recognition. Because they are reported to play essential roles in cellular control, there has been a special interest in the study of their structural and functional properties, yet the mechanisms by which they evolve to maintain functional interactions are poorly understood. By combining biophysical simulations of coarse-grained proteins and analysis of proteins-complex crystallographic structures, we seek to elucidate those mechanisms. We focus on two types of hub proteins: Multi hubs, which interact with their partners through different interfaces, and Singlish hubs, which do so through a single interface. We show that loss of structural stability is required for the evolution of protein-protein-interaction (PPI) networks, and it is more profound in Singlish hub systems. In addition, different ratios of hydrophobic to electrostatic interfacial amino acids are shown to support distinct network topologies (i.e., Singlish and Multi systems), and therefore underlie a fundamental design principle of PPI in a crowded environment. We argue that the physical nature of hydrophobic and electrostatic interactions, in particular, their favoring of either same-type interactions (hydrophobic-hydrophobic), or opposite-type interactions (negatively-positively charged) plays a key role in maintaining the network topology while allowing the protein amino acid sequence to evolve.
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