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Structure of insulin receptor substrate (IRS) proteins.77-81 IRS proteins are characterized by several structural domains. There is a high degree of
homology in the two domains in the N-terminal region of the proteins: pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains. The PH
domain binds polyphosphoinositides (e.g., phosphatidylinositol 3,4,-(bis)phosphate), and the PTB domain binds phosphotyrosine residues in the context of
Asn-Pro-Xaa-pTyr sequences. In addition, all four IRS proteins contain C-terminal sequences of varying lengths that contain multiple tyrosine
phosphorylation sites that represent binding sites for SH2 domains in various signaling proteins.
Source: Insulin Action, Insulin Resistance, and Type 2 Diabetes Mellitus, The Online Metabolic and Molecular Bases of Inherited Disease
Citation: Valle D, Beaudet AL, Vogelstein B, Kinzler KW, Antonarakis SE, Ballabio A, Gibson K, Mitchell G. The Online Metabolic and Molecular
Bases of Inherited Disease; 2014 Available at: http://mhmedical.com/ Accessed: August 03, 2017
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