Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
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DOI：
10.1126/science.275.5296.73
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发表时间：
1997-01-03
期刊：
影响因子：
56.9
通讯作者：
Cantley, LC
中科院分区：
文献类型：
--
作者：
Songyang, Z;Fanning, AS;Cantley, LC
定向肽库技术用于研究九个PDZ结构域的肽结合特异性。每个 PDZ 结构域选择在羧基末端具有疏水残基的肽。各个 PDZ 结构域选择了独特的最佳基序，主要由肽的羧基末端 3 至 7 个残基定义。 PDZ 结构域家族，包括 Discs Large 蛋白的结构域，选择了在羧基末端具有共有基序 Glu-(Ser/Thr)-Xxx-(Val/Ile)（其中 Xxx 代表任何氨基酸）的肽。相反，另一组PDZ结构域，包括LIN-2、p55和Tiam-1，选择在羧基末端三个残基处具有疏水性或芳香族侧链的肽。根据 PSD-95-3 PDZ 结构域的晶体结构，可以合理化用肽库观察到的特异性。
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 ami no acid) at the carboxyl terminus. in contrast, another ami ly 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.