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The PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signaling.

Authors: Moncoq, Karine  Broutin, Isabelle  Larue, Valéry  Perdereau, Dominique  Cailliau, Katia  Browaeys-Poly, Edith  Burnol, Anne-Françoise  Ducruix, Arnaud 
Citation: Moncoq K, etal., FEBS Lett. 2003 Nov 20;554(3):240-6.
Pubmed: (View Article at PubMed) PMID:14623073

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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CRRD Object Information
CRRD ID: 12793049
Created: 2017-03-18
Species: All species
Last Modified: 2017-03-18
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.