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Low-affinity protein-protein interactions (PPI) between domains of modular proteins and short,solvent-exposed peptide sequences within their binding partners play an essential role in intracellular signaling.An important class of PPIs are proline-rich motifs (PRM) that are spefically recognized by PRM-binding domains (PRD).Aromatic side chains of the PRDs define the binding pockets that often recognize individual proline residues while flanking sequences mediate specificity.Several of these PRM:PRD interactions are associated with cellular malfunction,cancer or infectious diseases.Thus,defining the impact of inhibiting PRS:PRD interactions on macromolecular complex assembly is an important step in establishing the interaction partners as potential drug targets.In this talk I will describe the molecular basis of PRM:PRD interactions,highlight their functional role in certain cellular processes and give an overview of recent strategies of inhibitor design.