Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks.

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.