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. 2008 Jun 21;7:19. doi: 10.1186/1475-2840-7-19

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Copyright © 2008 Shehata; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Structural Determinants of Insulin Receptor Substrates. IRS-1 and -2 are considerably similar in their general architecture [23,24,38]. They are composed of an NH2-terminal, pleckstrin homology (PH) domain that binds to membrane phospholipids, a phosphotyrosine binding (PTB) domain located just upstream the PH domain and is involved in the recognition of the asparagines-proline-glutamic acid-phosphotyrosine (NPEpY) sequence located in the juxtamembrane region of the insulin receptor β subunit, phosphoserine binding domain (PSB), and a less conserved COOH-terminal portion with multiple tyrosine phosphorylation motifs that can bind to specific SH2 domain-containing proteins.