Sandbox Reserved 1124: Difference between revisions
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==== The SH2 domain ==== | ==== The SH2 domain ==== | ||
This domain is very essential for the function of Grb2. In fact, <scene name='71/719865/Sh2domains/1'>the SH2 domain</scene> of Grb2 enables the interaction with receptors, scaffold proteins, tyrosine kinases but also with other adaptor proteins. Indeed, Shc is an intermediate between some receptors and Grb2. | This domain is very essential for the function of Grb2. In fact, <scene name='71/719865/Sh2domains/1'>the SH2 domain</scene> of Grb2 enables the interaction with receptors, scaffold proteins, tyrosine kinases but also with other adaptor proteins. Indeed, Shc is an intermediate between some receptors and Grb2.<ref name="polyprolin"/> | ||
The central SH2 domain binds growth factor receptors (EGFR or PDGFR) or scaffold proteins. When the SH2 domain of Grb2 binds to a receptor, the ability of the SH3 domains to interact with Sos motifs does not change.<ref > The Biochemistry of Cell Signalling, Ernst J. M. Helmreich, 2001, p.52 [https://global.oup.com/academic/product/the-biochemistry-of-cell-signalling-9780198508205?cc=fr&lang=en&]</ref> SH2 interacts preferentially with a tyrosine phosphorylated sequence with the following motif: pY-X-N-X (X is a hydrophobic residue).<ref > DOI:10.1371/journal.pone.0074482</ref>. Other non-receptor tyrosine kinases have also this motif and interact with Grb2 SH2 domain, such as BCR-Abl, focal adhesion kinase, insulin receptor substrate 1 and PTPN11.<ref name="A"/> | The central SH2 domain binds growth factor receptors (EGFR or PDGFR) or scaffold proteins. When the SH2 domain of Grb2 binds to a receptor, the ability of the SH3 domains to interact with Sos motifs does not change.<ref > The Biochemistry of Cell Signalling, Ernst J. M. Helmreich, 2001, p.52 [https://global.oup.com/academic/product/the-biochemistry-of-cell-signalling-9780198508205?cc=fr&lang=en&]</ref> SH2 interacts preferentially with a tyrosine phosphorylated sequence with the following motif: pY-X-N-X (X is a hydrophobic residue).<ref > DOI:10.1371/journal.pone.0074482</ref>. Other non-receptor tyrosine kinases have also this motif and interact with Grb2 SH2 domain, such as BCR-Abl, focal adhesion kinase, insulin receptor substrate 1 and PTPN11.<ref name="A"/> | ||
