Protein-protein binding selectivity and network topology constrain global and local properties of interface binding networks.

ABSTRACT: Protein-protein interactions networks (PPINs) are known to share a highly conserved structure across all organisms. What is poorly understood, however, is the structure of the child interface interaction networks (IINs), which map the binding sites proteins use for each interaction. In this study we analyze four independently constructed IINs from yeast and humans and find a conserved structure of these networks with a unique topology distinct from the parent PPIN. Using an IIN sampling algorithm and a fitness function trained on the manually curated PPINs, we show that IIN topology can be mostly explained as a balance between limits on interface diversity and a need for physico-chemical binding complementarity. This complementarity must be optimized both for functional interactions and ag

SUBMITTER: Holland DO 

PROVIDER: S-EPMC5514078 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature