Recognition of unique carboxyl-terminal motifs by distinct PDZ domains Academic Article Article uri icon


MeSH Major

  • Fatty Acids
  • Neoplasms


  • The oriented peptide library technique was used to investigate the peptide-binding specificities of nine PDZ domains. Each PDZ domain selected peptides with hydrophobic residues at the carboxyl terminus. Individual PDZ domains selected unique optimal motifs defined primarily by the carboxyl terminal three to seven residues of the peptides. One family of PDZ domains, including those of the Discs Large protein, selected peptides with the consensus motif Glu-(Ser/Thr)-Xxx-(Val/Ile) (where Xxx represents any amino acid) at the carboxyl terminus. In contrast, another family of PDZ domains, including those of LIN-2, p55, and Tiam-1, selected peptides with hydrophobic or aromatic side chains at the carboxyl terminal three residues. On the basis of crystal structures of the PSD-95-3 PDZ domain, the specificities observed with the peptide library can be rationalized.

publication date

  • January 3, 1997



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1126/science.275.5296.73

PubMed ID

  • 8974395

Additional Document Info

start page

  • 73

end page

  • 7


  • 275


  • 5296