Contextual specificity in peptide-mediated protein interactions.

ABSTRACT: Most biological processes 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. Although sufficient to ensure binding, these linear motifs alone are usually too short to achieve the high specificity observed, and additional contacts are often encoded in the residues surrounding the motif (i.e. the context). Here, we systematically identified all instances of peptide-mediated protein interactions of known three-dimensional structure and used them to investigate the individual contribution of motif and context to the global binding energy. We found that, on average, the context is responsible for roughly 20% of the binding and plays a crucial role

SUBMITTER: Stein A 

PROVIDER: S-EPMC2438476 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature