Functional genomics of intracellular peptide recognition domains with combinatorial biology methods
✍ Scribed by Sachdev S Sidhu; Gary D Bader; Charles Boone
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 147 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1367-5931
No coin nor oath required. For personal study only.
✦ Synopsis
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.