Functional genomics of intracellular peptide recognition domains with combinatorial biology methods

被引:20
作者
Sidhu, SS
Bader, GD
Boone, C
机构
[1] Genentech Inc, Dept Prot Engn, San Francisco, CA 94080 USA
[2] Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Toronto, ON M5S 1A8, Canada
[3] Univ Toronto, Dept Biochem, Toronto, ON M5G 1L6, Canada
[4] Univ Toronto, Banting & Best Dept Med Res, Toronto, ON M5G 1L6, Canada
[5] Univ Toronto, Dept Mol & Med Genet, Toronto, ON M5G 1L6, Canada
关键词
D O I
10.1016/S1367-5931(02)00011-x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Phage-displayed peptide libraries have been used to identify specific ligands for peptide-binding domains that mediate intracellular protein-protein interactions. These studies have provided significant insights into the specificities of particular domains. For PDZ domains that recognize C-terminal sequences, the information has proven useful in identifying natural binding partners from genomic databases. For SH3 domains that recognize internal proline-rich motifs, the results of database searches with phage-derived ligands have been compared with the results of yeast-two-hybrid experiments to produce overlap networks that reliably predict natural protein-protein interactions. In addition, libraries of phage-displayed PDZ and SH3 domains have been used to identify the residues responsible for ligand recognition, and also to engineer domains with altered specificities.
引用
收藏
页码:97 / 102
页数:6
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