The tetratricopeptide-repeat motif is a versatile platform that enables diverse modes of molecular recognition

•The most common interaction is a short, negatively-charged peptide binding across a groove formed by two to three TPRs.•Longer peptides bind in an extended conformation across ten or more TPRs, with much higher binding affinities resulting.•Other modes of high-affinity interaction include the binding of an extended peptide to a kinked bipartite TPR array.•Binding of TPRs to globular domains and homo-oligomerisation of TPRs further diversify their binding capabilities.•The scaffold may be suited to the binding of multiple partner proteins, enabling design of multi-functional TPR proteins.