Across-proteome modeling of dimer structures for the bottom-up assembly of protein-protein interaction networks.

ABSTRACT:

Background

Deciphering complete networks of interactions between proteins is the key to comprehend cellular regulatory mechanisms. A significant effort has been devoted to expanding the coverage of the proteome-wide interaction space at molecular level. Although a growing body of research shows that protein docking can, in principle, be used to predict biologically relevant interactions, the accuracy of the across-proteome identification of interacting partners and the selection of near-native complex structures still need to be improved.

Results

In this study, we developed a new method to discover and model protein interactions employing an exhaustive all-to-all docking strategy. This approach integrates molecular modeling, structural bioinformatics, machine learning, and f

SUBMITTER: Maheshwari S 

PROVIDER: S-EPMC5427563 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature