An adjacent arginine, and the phosphorylated tyrosine in the c-Met receptor target sequence, dictates the orientation of c-Cbl binding.
FEBS Lett
; 585(2): 281-5, 2011 Jan 21.
Article
em En
| MEDLINE
| ID: mdl-21163258
ABSTRACT
Previously, we have demonstrated that the tyrosine phosphorylated hepatocyte growth factor receptor (Met) binds to the c-Cbl phosphotyrosine-recognition, tyrosine kinase binding (TKB) domain in a reverse orientation compared to other c-Cbl binding partners. A Met peptide with the DpYR motif changed to RpYD (MetRD) retains a similar TKB binding affinity as the native Met peptide. However, the TKB MetRD complex crystal structure reveals a complete reversal of the binding orientation. Collated data indicates that both binding and orientation is dictated by the phosphorylated tyrosine and an adjacent arginine forming intra-peptide hydrogen bonds and aligning unidirectionally with complementary charges in the phosphotyrosine binding pocket of c-Cbl.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Arginina
/
Receptores de Fatores de Crescimento
/
Fosfotirosina
/
Proteínas Proto-Oncogênicas c-met
/
Proteínas Proto-Oncogênicas c-cbl
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Singapura