The multiple-specificity landscape of modular peptide recognition domains.

ABSTRACT: Modular protein interaction domains form the building blocks of eukaryotic signaling pathways. Many of them, known as peptide recognition domains, mediate protein interactions by recognizing short, linear amino acid stretches on the surface of their cognate partners with high specificity. Residues in these stretches are usually assumed to contribute independently to binding, which has led to a simplified understanding of protein interactions. Conversely, we observe in large binding peptide data sets that different residue positions display highly significant correlations for many domains in three distinct families (PDZ, SH3 and WW). These correlation patterns reveal a widespread occurrence of multiple binding specificities and give novel structural insights into protein interactions. For e

SUBMITTER: Gfeller D 

PROVIDER: S-EPMC3097085 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature