Proline-rich sequence recognition domains (PRD): ligands, function and inhibition.

@article{Freund2008ProlinerichSR,
  title={Proline-rich sequence recognition domains (PRD): ligands, function and inhibition.},
  author={Christian Freund and H-G Schmalz and Jana Sticht and Ronald K{\"u}hne},
  journal={Handbook of experimental pharmacology},
  year={2008},
  volume={186},
  pages={407-29}
}
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 comprises proline-rich motifs (PRM) that are specifically 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… CONTINUE READING

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