Evolving specificity from variability for protein interaction domains.
Trends Biochem Sci
; 36(4): 183-90, 2011 Apr.
Article
em En
| MEDLINE
| ID: mdl-21227701
ABSTRACT
An important question in modular domain-peptide interactions, which play crucial roles in many biological processes, is how the diverse specificities exhibited by different members of a domain family are encoded in a common scaffold. Analysis of the Src homology (SH) 2 family has revealed that its specificity is determined, in large part, by the configuration of surface loops that regulate ligand access to binding pockets. In a distinct manner, SH3 domains employ loops for ligand recognition. The PDZ domain, in contrast, achieves specificity by co-evolution of binding-site residues. Thus, the conformational and sequence variability afforded by surface loops and binding sites provides a general mechanism by which to encode the wide spectrum of specificities observed for modular protein interaction domains.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Domínios e Motivos de Interação entre Proteínas
Limite:
Humans
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article