Molecular recognition of protein surfaces: high affinity ligands for the CBP KIX domain.

ABSTRACT: Potent and specific inhibitors of protein.protein interactions have potential both as therapeutic compounds and biological tools, yet discovery of such molecules remains a challenge. Our laboratory has recently described a strategy, called protein grafting, for the identification of miniature proteins that bind protein surfaces with high affinity and specificity and inhibit the formation of protein.protein complexes. In protein grafting, those residues that comprise a functional alpha-helical binding epitope are stabilized on the solvent-exposed alpha-helical face of the small yet stable protein avian pancreatic polypeptide (aPP). Here we use protein grafting in combination with molecular evolution by phage display to identify phosphorylated peptide ligands that recognize the shallow surfa

SUBMITTER: Rutledge SE 

PROVIDER: S-EPMC2926944 | biostudies-literature | 2003 Nov

REPOSITORIES: biostudies-literature