Triangle network motifs predict complexes by complementing high-error interactomes with structural information.

ABSTRACT:

Background

A lot of high-throughput studies produce protein-protein interaction networks (PPINs) with many errors and missing information. Even for genome-wide approaches, there is often a low overlap between PPINs produced by different studies. Second-level neighbors separated by two protein-protein interactions (PPIs) were previously used for predicting protein function and finding complexes in high-error PPINs. We retrieve second level neighbors in PPINs, and complement these with structural domain-domain interactions (SDDIs) representing binding evidence on proteins, forming PPI-SDDI-PPI triangles.

Results

We find low overlap between PPINs, SDDIs and known complexes, all well below 10%. We evaluate the overlap of PPI-SDDI-PPI triangles with known complexes from Munich In

SUBMITTER: Andreopoulos B 

PROVIDER: S-EPMC2714575 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature