Abstract
Src Homology 2 (SH2) domains are small modular domains found within a great number of proteins involved in different signaling pathways. They are able to bind specific motifs containing a phopshorylated tyrosine residue, propagating the signal downstream promoting protein-protein interaction and/or modifying enzymatic activities. Different families of SH2 domains may have different binding specifity, which is usually determined by few residues C-terminal with respect to the pY (positions +1, +2 and +3. Non-phosphorylated peptides do not bind to the SH2 domains. At least three different binding motifs are known: pYEEI (Src-family SH2 domains), pY[IV].[VILP] (SH-PTP2, phospholipase C-gamma), pY.[EN] (GRB2). The interaction between SH2 domains and their substrates is however dependent also to cooperative contacts of other surface regions.
Selected references
| Wang X, Darus CJ, Xu BC, Kopchick JJ | | Identification of growth hormone receptor (GHR) tyrosine residues required
for GHR phosphorylation and JAK2 and STAT5 activation. | | Mol Endocrinol 1996 Oct;10(10) : 1249-60. | | PMID: 9121492 |
This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.
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Biological Process |
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Cellular Component |
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cytosol |
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Molecular Function |
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SH2-domain binding |
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