Sandbox Reserved 1124: Difference between revisions
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===The SH2 domain=== | ===The SH2 domain=== | ||
<scene name='71/719865/Sh2domains/1'>The SH2 domain</scene> encompasses 8 beta strands (61 to 64 ; 82 to 87 ; 95 to 101 ; 104 to 109 ; 111 to 112 ; 118 to 119 ; 124 to 125 ; 149 - 150) and 2 alpha helices (67 to 74 and 128 to 134). The βB, βC and βD strands compose a three-stranded antiparallel β-sheet and the 2 α-helices are positioned on both sides. Moreover, the short parallel βA and βG strands extend the central β-sheet. There are also βD', βE and βF strands which are smaller β-sheet-like structure. <ref>DOI:10.1007/s10858-008-9272-0</ref> | <scene name='71/719865/Sh2domains/1'>The SH2 domain</scene> encompasses 8 beta strands (61 to 64 ; 82 to 87 ; 95 to 101 ; 104 to 109 ; 111 to 112 ; 118 to 119 ; 124 to 125 ; 149 - 150) and 2 alpha helices (67 to 74 and 128 to 134). The βB, βC and βD strands compose a three-stranded antiparallel β-sheet and the 2 α-helices are positioned on both sides. Moreover, the short parallel βA and βG strands extend the central β-sheet. There are also βD', βE and βF strands which are smaller β-sheet-like structure. <ref>DOI:10.1007/s10858-008-9272-0</ref> [[Image:Sequence_of_the_SH2_domain_of_Grb2.PNG | thumb | upright=3 | Sequence of the SH2 domain (60 to 152 amino acids) of Grb2]] | ||
[[Image:Sequence_of_the_SH2_domain_of_Grb2.PNG | thumb | upright=3 | Sequence of the SH2 domain (60 to 152 amino acids) of Grb2]] | |||
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 abolish the phosphotyrosine dependent interactions.<ref>Kousik Kundu In Silico Prediction of Modular Domain-Peptide Interactions (2015) [https://scholar.google.com/citations?view_op=view_citation&hl=en&user=0iOlQDAAAAAJ&citation_for_view=0iOlQDAAAAAJ:qUcmZB5y_30C]</ref> | 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 abolish the phosphotyrosine dependent interactions.<ref>Kousik Kundu In Silico Prediction of Modular Domain-Peptide Interactions (2015) [https://scholar.google.com/citations?view_op=view_citation&hl=en&user=0iOlQDAAAAAJ&citation_for_view=0iOlQDAAAAAJ:qUcmZB5y_30C]</ref> | ||
