Sandbox Reserved 1124: Difference between revisions

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The amino acid in red are residues which are responsible for forming the phosphopeptide binding pocket. In green, this is residues which can bind to the negatively charged phosphorylated tyrosine residue of the binding peptide. This domain is very essential for the function of Grb2. Actually, several mutations in the SH2 domains can cause human diseases. A mutation for example of the arginin residue at position 5 of βB can cancel the phosphotyrosine dependent interactions.<ref name="Kousik"/>
The amino acid in red are residues which are responsible for forming the phosphopeptide binding pocket. In green, these are residues which can bind to the negatively charged phosphorylated tyrosine residue of the binding peptide. This domain is very essential for the function of Grb2. Actually, several mutations in the SH2 domains can cause human diseases. A mutation for example of the arginin residue at position 5 of βB can cancel the phosphotyrosine dependent interactions.<ref name="Kousik"/>
The SH2 domain 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.
The SH2 domain 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.