FEBS Letters · 2006 · 299 citations · 23 references
Life SciencesBiochemistryBioinformaticsProtein-protein InteractionsStructural BioinformaticsStructural BiologyProtein Complex Structure PredictionProtein Interaction DomainsProtein StructureProtein-protein Interaction AnalysisProtein-protein Interaction ModelingProtein-protein Interaction NetworksDisorder In Multivalent InteractionsFlexibilityProtein Interaction Network TopologyProtein Surface ElectrostaticsProtein Topology EffectsProtein-protein Interaction DomainsProtein-protein Interactions In Disordered ProteinsSurface Charge Properties
We investigate the structural properties of hubs that enable them to interact with several partners in protein-protein interaction networks. We find that hubs have more observed and predicted disordered residues with fewer loops/coils, and more charged residues on the surface as compared to non-hubs. Smaller hubs have fewer disordered residues and more charged residues on the surface than larger hubs. We conclude that the global flexibility provided by disordered domains, and high surface charge are complementary factors that play a significant role in the binding ability of hubs.
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