Characterization of Diverse Internal Binding Specificities of PDZ Domains by Yeast Two-Hybrid Screening of a Special Peptide Library

摘要: Protein-protein interactions (PPIs) are essential events to play important roles in a series of biological processes. There probably more ways PPIs than we currently realized. Structural and functional investigations weak have lagged behind those strong due technical difficulties. Weak often short-lived, which may result dynamic signals with within and/or between cells. For example, the characteristics PSD-95/Dlg/ZO-1 (PDZ) domain binding internal sequences, primarily interactions, not yet been systematically explored. In present study, constructed nearly random octapeptide yeast two-hybrid library. A total 24 PDZ domains were used as baits for screening Fourteen these able bind PDZ-domain motifs (PBMs), PBMs screened nine exhibited preferences. Among 11 that reported their PBM ability, six confirmed PBMs. The first LNX2, has C-terminal PBMs, was found These results suggest ability underestimated. data provided diverse properties several help identify novel partners.