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XB-ART-4411
FEBS Lett 2003 Nov 20;5543:240-6. doi: 10.1016/s0014-5793(03)01095-0.
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The PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signaling.

Moncoq K , Broutin I , Larue V , Perdereau D , Cailliau K , Browaeys-Poly E , Burnol AF , Ducruix A .


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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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Species referenced: Xenopus laevis
Genes referenced: grb14 grb7 ins pir