Characterization of diverse internal binding specificities of PDZ domains by yeast two-hybrid screening of a special peptide library.

ABSTRACT: Protein-protein interactions (PPIs) are essential events to play important roles in a series of biological processes. There are probably more ways of PPIs than we currently realized. Structural and functional investigations of weak PPIs have lagged behind those of strong PPIs due to technical difficulties. Weak PPIs are often short-lived, which may result in more dynamic signals with important biological roles within and/or between cells. For example, the characteristics of PSD-95/Dlg/ZO-1 (PDZ) domain binding to internal sequences, which are primarily weak interactions, have not yet been systematically explored. In the present study, we constructed a nearly random octapeptide yeast two-hybrid library. A total of 24 PDZ domains were used as baits for screening the library. Fourteen of thes

SUBMITTER: Mu Y 

PROVIDER: S-EPMC3913781 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature