Transient association between proteins elicits alteration of dynamics at sites far away from interfaces

Proteins are known to undergo structural changes upon binding to partner proteins. However, the prevalence, extent, location, and function of change in protein dynamics due to transient protein-protein interactions is not well documented. Here, we have analyzed a dataset of 58 protein-protein complexes of known three-dimensional structure and structures of their corresponding unbound forms to evaluate dynamics changes induced by binding. Fifty-five percent of cases showed significant dynamics change away from the interfaces. This change is not always accompanied by an observed structural change. Binding of protein partner is found to alter inter-residue communication within the tertiary structure in about 90% of cases. Also, residue motions accessible to proteins in unbound form were not always maintained in the bound form. Further analyses revealed functional roles for the distant site where dynamics change was observed. Overall, the results presented here strongly suggest that alteration of protein dynamics due to binding of a partner protein commonly occurs.

Automated summary

Analysis of 58 protein-protein complexes revealed that approximately 55% of cases showed significant dynamics change upon binding, even without accompanying structural change. Binding of a protein partner was found to alter inter-residue communication within the tertiary structure in about 90% of cases, and accessible residue motions in unbound proteins were not always maintained in the bound form. Overall, the results strongly suggest that alteration of protein dynamics due to binding is a common occurrence.