Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains
| Autor: | Lewis C. Cantley, Athar H. Chishti, C. Fu, Shirin M. Marfatia, Zhou Songyang, Alan S. Fanning, James M. Anderson, Jian Xu, Anne M. Crompton, Andrew C. Chan |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular PDZ domain Kinesins Nerve Tissue Proteins Peptide Myosins Biology Membrane-associated guanylate kinase Crystallography X-Ray Protein Structure Secondary Protein structure Peptide Library Animals Guanine Nucleotide Exchange Factors Humans T-Lymphoma Invasion and Metastasis-inducing Protein 1 Amino Acid Sequence Binding site Peptide library Peptide sequence chemistry.chemical_classification Binding Sites Multidisciplinary Sequence Homology Amino Acid Membrane Proteins Proteins Helminth Proteins Protein Structure Tertiary Amino acid chemistry Biochemistry Protein Tyrosine Phosphatases Nucleoside-Phosphate Kinase Peptides Guanylate Kinases |
| Zdroj: | Science. 275:73-77 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.275.5296.73 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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