Design of protein-interaction specificity gives selective bZIP-binding peptides.

ABSTRACT: Interaction specificity is a required feature of biological networks and a necessary characteristic of protein or small-molecule reagents and therapeutics. The ability to alter or inhibit protein interactions selectively would advance basic and applied molecular science. Assessing or modelling interaction specificity requires treating multiple competing complexes, which presents computational and experimental challenges. Here we present a computational framework for designing protein-interaction specificity and use it to identify specific peptide partners for human basic-region leucine zipper (bZIP) transcription factors. Protein microarrays were used to characterize designed, synthetic ligands for all but one of 20 bZIP families. The bZIP proteins share strong sequence and structural simi

SUBMITTER: Grigoryan G 

PROVIDER: S-EPMC2748673 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature