Specialized Dynamical Properties of Promiscuous Residues Revealed by Simulated Conformational Ensembles.

ABSTRACT: The ability to interact with different partners is one of the most important features in proteins. Proteins that bind a large number of partners (hubs) have been often associated with intrinsic disorder. However, many examples exist of hubs with an ordered structure, and evidence of a general mechanism promoting promiscuity in ordered proteins is still elusive. An intriguing hypothesis is that promiscuous binding sites have specific dynamical properties, distinct from the rest of the interface and pre-existing in the protein isolated state. Here, we present the first comprehensive study of the intrinsic dynamics of promiscuous residues in a large protein data set. Different computational methods, from coarse-grained elastic models to geometry-based sampling methods and to full-atom Molecul

SUBMITTER: Fornili A 

PROVIDER: S-EPMC3827836 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature