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Domain binding and function: Src-homology 2 (SH2) domains are modules of ~100 amino acids that bind to specific phospho (pY)-containing peptide motifs. Conventional SH2 domains have a conserved pocket that recognizes pY, and a more variable pocket that binds 3-6 residues C-terminal to the pY and confers specificity. The SAP SH2 domain recognizes Y as well as pY in the context of residues N and C terminal, suggesting an alternate 3-pronged model may apply in some cases. Phosphopeptides of optimal sequence bind to SH2 domains with dissociation constants of ~50-500 nM. Structure Reference: Waksman, G. et al. (1993) Cell 72(5): 779-90.
Examples of Domain Proteins:
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Binding Examples:
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SH2 domain proteins |  |
Binding partners | Phosphopeptide Ligand | |
SH2 specificity residues |  | |
| Src Tyrosine Kinase | Focal Adhesion Kinase | pTyr-Ala-Glu-Ile | Tyr betaD5 | |||||
| Phospho-lipase C-gamma C-terminal SH2 | betaPDGF-receptor | pTyr-Ile-Ile-Pro-Leu-Pro-Asp | Cys betaD5 | |||||
| Grb2 adaptor | Shc docking protein | pTyr-Val-Asn-Val ____ _______________ | | Regulation Specificity |
Trp EF1 |
