Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
作者： Z Songyang , AS Fanning , C Fu , J Xu , SM Marfatia
DOI: 10.1126/SCIENCE.275.5296.73
关键词:
摘要: The oriented peptide library technique was used to investigate the peptide-binding specificities of nine PDZ domains. Each domain selected peptides with hydrophobic residues at carboxyl terminus. Individual domains unique optimal motifs defined primarily by terminal three seven peptides. One family domains, including those Discs Large protein, consensus motif Glu-(Ser/Thr)-Xxx-(Val/Ile) (where Xxx represents any amino acid) In contrast, another LIN-2, p55, and Tiam-1, or aromatic side chains residues. On basis crystal structures PSD-95-3 domain, observed can be rationalized.
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