Correction: SLiMEnrich: computational assessment of protein-protein interaction data as a source of domain-motif interactions.

Sobia Idrees,Åsa Pérez-Bercoff,Richard J Edwards

doi:10.7717/peerj.5858/correction-1

Abstract

[This corrects the article DOI: 10.7717/peerj.5858.].

Highlights

Proteins interact with their partners through two main classes of functional modules: globular domains and Short Linear Motifs (SLiMs) (Bhattacharyya et al, 2006)
SLiMEnrich analysis revealed the case study Y2H data to be enriched for domain-motif interactions (DMIs) under all DMI prediction strategies (Fig. 5, Table 1)
There are many data- and method-specific factors that will determine whether protein– protein interaction (PPI) data are useful for short linear motif (SLiM) prediction

Summary

Introduction

Proteins interact with their partners through two main classes of functional modules: globular domains and Short Linear Motifs (SLiMs) (Bhattacharyya et al, 2006). SLiMs are short protein regions (typically 3–10 amino acids long) with a small number of key residues that mediate domain-motif interactions (DMIs) with the globular domain of a protein–protein interaction (PPI) partner (Davey et al, 2012). These DMIs underpin critical cellular functions, including cell cycle regulation, cell compartment targeting, post-translational modification, protein degradation, and signal transduction. This was used as evidence that many more SLiMs and DMI are yet to be discovered, and raises concerns that these methods are depleted for DMIs

Methods

Results

Discussion

Conclusion