Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display.
J Biol Chem
; 275(28): 21486-91, 2000 Jul 14.
Article
em En
| MEDLINE
| ID: mdl-10887205
ABSTRACT
PDZ domains mediate protein-protein interactions at specialized subcellular sites, such as epithelial cell tight junctions and neuronal post-synaptic densities. Because most PDZ domains bind extreme carboxyl-terminal sequences, the phage display method has not been amenable to the study of PDZ domain binding specificities. For the first time, we demonstrate the functional display of a peptide library fused to the carboxyl terminus of the M13 major coat protein. We used this library to analyze carboxyl-terminal peptide recognition by two PDZ domains. For each PDZ domain, the library provided specific ligands with sub-micromolar binding affinities. Synthetic peptides and homology modeling were used to dissect and rationalize the binding interactions. Our results establish carboxyl-terminal phage display as a powerful new method for mapping PDZ domain binding specificity.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Capsídeo
/
Biblioteca de Peptídeos
/
Proteínas do Capsídeo
/
Proteínas de Membrana
/
Proteínas do Tecido Nervoso
Limite:
Humans
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2000
Tipo de documento:
Article