Disordered binding regions and linear motifs--bridging the gap between two models of molecular recognition.

ABSTRACT: Intrinsically disordered proteins (IDPs) exist without the presence of a stable tertiary structure in isolation. These proteins are often involved in molecular recognition processes via their disordered binding regions that can recognize partner molecules by undergoing a coupled folding and binding process. The specific properties of disordered binding regions give way to specific, yet transient interactions that enable IDPs to play central roles in signaling pathways and act as hubs of protein interaction networks. An alternative model of protein-protein interactions with largely overlapping functional properties is offered by the concept of linear interaction motifs. This approach focuses on distilling a short consensus sequence pattern from proteins with a common interaction partner. Th

SUBMITTER: Meszaros B 

PROVIDER: S-EPMC3463566 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature