ArticleCell reports2018
Ligand Binding Site Structure Influences the Evolution of Protein Complex Function and Topology.
Article in Cell reports, 2018. 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, 31 citations in OpenAlex.
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- Structural variability of multifunctional proteins indicates frequent stochastic evolution of protein oligomers.Communications biology · 2025Article
- Systematic Exploration of Small-Molecule Binding via a Large Language Model Trained on Textualized Protein-Ligand Interactions.Molecules (Basel, Switzerland) · 2025Article
- Human Coronavirus-229E Hijacks Key Host-Cell RNA-Processing Complexes for Replication.Journal of proteome research · 2025Article
- Cellular location shapes quaternary structure of enzymes.Nature communications · 2024Article
- An Assessment of Quaternary Structure Functionality in Homomer Protein Complexes.Molecular biology and evolution · 2023Article
- It's ok to be outnumbered - sub-stoichiometric modulation of homomeric protein complexes.RSC medicinal chemistry · 2023Review
- Defining A Global Map of Functional Group-based 3D Ligand-binding Motifs.Genomics, proteomics & bioinformatics · 2022Article
- Insights into the genes involved in the ethylene biosynthesis pathway in Arabidopsis thaliana and Oryza sativa.Journal, genetic engineering & biotechnology · 2020Article
- Similarities in biological processes can be used to bridge ecology and molecular biology.Evolutionary applications · 2020Article
- Recent advances suggest increased influence of selective pressure in allostery.Current opinion in structural biology · 2020Review
- Ligands and Receptors with Broad Binding Capabilities Have Common Structural Characteristics: An Antibiotic Design Perspective.Journal of medicinal chemistry · 2019Review
- Evolution of (p)ppGpp-HPRT regulation through diversification of an allosteric oligomeric interaction.eLife · 2019Article
- Ligand Binding Site Structure Shapes Folding, Assembly and Degradation of Homomeric Protein Complexes.Journal of molecular biology · 2019Article
- Ligand-Binding-Site Structure Shapes Allosteric Signal Transduction and the Evolution of Allostery in Protein Complexes.Molecular biology and evolution · 2019Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
It has been suggested that the evolution of protein complexes is significantly influenced by stochastic, non-adaptive processes. Using ligand binding as a proxy of function, we show that the structure of ligand-binding sites significantly influences the evolution of protein complexes. We show that homomers with multi-chain binding sites (MBSs) evolve new functions slower than monomers or other homomers, and those binding cofactors and metals have more conserved quaternary structure than other homomers. Moreover, the ligands and ligand-binding pockets of homologous MBS homomers are more similar than monomers and other homomers. Our results suggest strong evolutionary selection for quaternary structure in cofactor-binding MBS homomers, whereas neutral processes are more important in complexes with single-chain binding sites. They also have pharmacological implications, suggesting that complexes with single-chain binding sites are better targets for selective drugs, whereas MBS homomers are good candidates for broad-spectrum antibiotic and multitarget drug design.
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