src homology 2 [SH2] domain

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Introduction

A group of related sequences 50-100 amino acids in length. SH2-domains bind to tyrosine phosphates with specificity of different SH2-domains for different phosphotyrosine motifs. Their probable function is to modulate protein-protein interactions of tyrosine-phosphorylated proteins, largely by colocalizing the proteins involved in the pTyr-SH2 interaction. The specificity of SH2-domains for specific tyrosine phosphates is determined by variable residues in the SH2-domain & residues C-terminal to the phosphorylated tyrosine.

Kd is 10-100 nM for high affinity binding. The only invariant residue in SH2 domains is an Arg which forms hydrogen bonds with 2 pTyr oxygens. The Arg is frequently contained within a FLVRES motif, a Ser phosphorylation site in which phosphorylation may inhibit SH2-pTyr interactions.

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References

  1. Ellis C, Moran M, McCormick F, Pawson T. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature. 1990 Jan 25;343(6256):377-81. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1689011
  2. Matsuda M, Mayer BJ, Fukui Y, Hanafusa H. Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science. 1990 Jun 22;248(4962):1537-9. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1694307
  3. Saikumar P, Murali R, Reddy EP. Role of tryptophan repeats and flanking amino acids in Myb-DNA interactions. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8452-6. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2236054
  4. Pawson T Protein modules and signalling networks Nature 373:573 1995 (Notch) PMID: https://www.ncbi.nlm.nih.gov/pubmed/7531822