Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold.

ABSTRACT: An improved knowledge of protein-protein interactions is essential for better understanding of metabolic and signaling networks, and cellular function. Progress tends to be based on structure determination and predictions using known structures, along with computational methods based on evolutionary information or detailed atomistic descriptions. We hypothesized that for the case of interactions across a common interface, between proteins from a pair of paralogue families or within a family of paralogues, a relatively simple interface description could distinguish between binding and non-binding pairs. Using binding data for several systems, and large-scale comparative modeling based on known template complex structures, it is found that charge-charge interactions (for groups bearing net c

SUBMITTER: Ivanov SM 

PROVIDER: S-EPMC5634604 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature