The PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signaling.
FEBS Lett
; 554(3): 240-6, 2003 Nov 20.
Article
em En
| MEDLINE
| ID: mdl-14623073
ABSTRACT
Grb14 belongs to the Grb7 family of adapter proteins and was identified as a negative regulator of insulin signal transduction. Its inhibitory effect on the insulin receptor kinase activity is controlled by a newly discovered domain called PIR. To investigate the biochemical and biophysical characteristics of this new domain, we cloned and purified recombinant PIR-SH2, PIR, and SH2 domains. The isolated PIR and PIR-SH2 domains were physiologically active and inhibited insulin-induced reinitiation of meiosis in the Xenopus oocytes system. However, NMR experiments on (15)N-labelled PIR revealed that it did not present secondary structure. These results suggest that the PIR domain belongs to the growing family of intrinsically unstructured proteins.
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Base de dados:
MEDLINE
Assunto principal:
Receptor de Insulina
/
Proteínas
/
Proteínas de Xenopus
/
Insulina
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
França