The SH2 domain is a small protein domain that occurs in eukaryotic cells, where it performs important functions in signal transduction. It consists of about 100 amino acids. SH2 stands for "Src-homology 2". The SH2 domain represents a binding motif consisting of about 100 amino acid residues that binds to substrate proteins with high affinity and specificity, whereby their SH2 binding site consists only of a phosphorylated tyrosine residue and a few neighbouring amino acid residues.
SH2-domain
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In the context of signal transduction, the SH2 domain is essential for the control of signaling proteins such as:
- C-Src
- C-Abl (oncogenes)
- Phosphotyrosyl protein phosphatases
- Cγ phospholipase
- GAP (GTPase-activating proteins).
- Phosphoinositide 3-kinases