ArticlePLoS computational biology2012
Versatility and invariance in the evolution of homologous heteromeric interfaces.
Article in PLoS computational biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Correlated Evolution Drives Structural Convergence of Interacting Proteins.Journal of molecular evolution · 2026Article
- Structural comparison of homologous protein-RNA interfaces reveals widespread overall conservation contrasted with versatility in polar contacts.PLoS computational biology · 2024Article
- Modularity and diversity of target selectors in Tn7 transposons.Molecular cell · 2023Article
- Structural and conformational changes induced by missense variants in the zinc finger domains of GATA3 involved in breast cancer.RSC advances · 2020Article
- Protein-peptide docking using CABS-dock and contact information.Briefings in bioinformatics · 2019Article
- Protein-protein interaction specificity is captured by contact preferences and interface composition.Bioinformatics (Oxford, England) · 2018Article
- The PHD finger protein Spp1 has distinct functions in the Set1 and the meiotic DSB formation complexes.PLoS genetics · 2018Article
- PDB-wide identification of biological assemblies from conserved quaternary structure geometry.Nature methods · 2018Article
- Article
- Conservation of coevolving protein interfaces bridges prokaryote-eukaryote homologies in the twilight zone.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A topological and conformational stability alphabet for multipass membrane proteins.Nature chemical biology · 2016Article
- Weak conservation of structural features in the interfaces of homologous transient protein-protein complexes.Protein science : a publication of the Protein Society · 2015Article
- Predicting the Effect of Mutations on Protein-Protein Binding Interactions through Structure-Based Interface Profiles.PLoS computational biology · 2015Article
- Molecular determinants of the DprA-RecA interaction for nucleation on ssDNA.Nucleic acids research · 2014Article
- Article
- Protein flexibility facilitates quaternary structure assembly and evolution.PLoS biology · 2014Article
- Article
- Structural templates for modeling homodimers.Protein science : a publication of the Protein Society · 2013Article
- A compact viral processing proteinase/ubiquitin hydrolase from the OTU family.PLoS pathogens · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Evolutionary pressures act on protein complex interfaces so that they preserve their complementarity. Nonetheless, the elementary interactions which compose the interface are highly versatile throughout evolution. Understanding and characterizing interface plasticity across evolution is a fundamental issue which could provide new insights into protein-protein interaction prediction. Using a database of 1,024 couples of close and remote heteromeric structural interologs, we studied protein-protein interactions from a structural and evolutionary point of view. We systematically and quantitatively analyzed the conservation of different types of interface contacts. Our study highlights astonishing plasticity regarding polar contacts at complex interfaces. It also reveals that up to a quarter of the residues switch out of the interface when comparing two homologous complexes. Despite such versatility, we identify two important interface descriptors which correlate with an increased conservation in the evolution of interfaces: apolar patches and contacts surrounding anchor residues. These observations hold true even when restricting the dataset to transiently formed complexes. We show that a combination of six features related either to sequence or to geometric properties of interfaces can be used to rank positions likely to share similar contacts between two interologs. Altogether, our analysis provides important tracks for extracting meaningful information from multiple sequence alignments of conserved binding partners and for discriminating near-native interfaces using evolutionary information.
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