The many faces of Ras: recognition of small GTP-binding proteins.
Trends Biochem Sci
; 26(12): 710-6, 2001 Dec.
Article
em En
| MEDLINE
| ID: mdl-11738594
ABSTRACT
The structures of over 30 complexes of Ras superfamily small GTP-binding proteins bound to diverse protein partners have been reported. Comparison of these complexes using the sequences of the small GTP-binding proteins to align the contact sites shows that virtually all surface positions make contacts with at least one partner protein. Rather than highlighting a single consensus binding site, these comparisons illustrate the remarkable diversity of contacts of Ras superfamily members. Here, a new analysis technique, the interface array, is introduced to quantify patterns of surface contacts. The interface array shows that small GTP-binding proteins are recognized in at least nine distinct ways. Remarkably, binding partners with similar functions, including those with distinct folds, recognize small GTP-binding proteins in similar ways. These classes of shared surface contacts support the occurrence of both divergent and convergent evolutionary processes and suggest that specific effector functions require particular protein-protein contacts.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Monoméricas de Ligação ao GTP
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Trends Biochem Sci
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Estados Unidos