SLiM-Enrich: computational assessment of protein-protein interaction data as a source of domain-motif interactions.

ABSTRACT: Many important cellular processes involve protein-protein interactions (PPIs) mediated by a Short Linear Motif (SLiM) in one protein interacting with a globular domain in another. Despite their significance, these domain-motif interactions (DMIs) are typically low affinity, which makes them challenging to identify by classical experimental approaches, such as affinity pulldown mass spectrometry (AP-MS) and yeast two-hybrid (Y2H). DMIs are generally underrepresented in PPI networks as a result. A number of computational methods now exist to predict SLiMs and/or DMIs from experimental interaction data but it is yet to be established how effective different PPI detection methods are for capturing these low affinity SLiM-mediated interactions. Here, we introduce a new computational pipeline (S

SUBMITTER: Idrees S 

PROVIDER: S-EPMC6215436 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature