Novel peptide-mediated interactions derived from high-resolution 3-dimensional structures.

ABSTRACT: Many biological responses to intra- and extracellular stimuli are regulated through complex networks of transient protein interactions where a globular domain in one protein recognizes a linear peptide from another, creating a relatively small contact interface. These peptide stretches are often found in unstructured regions of proteins, and contain a consensus motif complementary to the interaction surface displayed by their binding partners. While most current methods for the de novo discovery of such motifs exploit their tendency to occur in disordered regions, our work here focuses on another observation: upon binding to their partner domain, motifs adopt a well-defined structure. Indeed, through the analysis of all peptide-mediated interactions of known high-resolution three-dimension

SUBMITTER: Stein A 

PROVIDER: S-EPMC2873903 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature