 Crystallographic structure of the SH2 domain. The structure consists of a large beta sheet (green) flanked by two alpha-helices (orange and blue).[1] | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | SH2 | ||||||||
| Pfam | PF00017 | ||||||||
| InterPro | IPR000980 | ||||||||
| SMART | SH2 | ||||||||
| PROSITE | PDOC50001 | ||||||||
| SCOP2 | 1sha / SCOPe / SUPFAM | ||||||||
| CDD | cd00173 | ||||||||
| |||||||||
The SH2 (Src Homology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein[2] and in many other intracellular signal-transducing proteins.[3] SH2 domains bind to phosphorylated tyrosine residues on other proteins, modifying the function or activity of the SH2-containing protein. The SH2 domain may be considered the prototypical modular protein-protein interaction domain, allowing the transmission of signals controlling a variety of cellular functions.[4] SH2 domains are especially common in adaptor proteins that aid in the signal transduction of receptor tyrosine kinase pathways.[5]
- ^ PDB: 1lkk; Tong L, Warren TC, King J, Betageri R, Rose J, Jakes S (March 1996). "Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution". Journal of Molecular Biology. 256 (3): 601–10. doi:10.1006/jmbi.1996.0112. PMID 8604142.
- ^ Sadowski I, Stone JC, Pawson T (December 1986). "A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps". Molecular and Cellular Biology. 6 (12): 4396–408. doi:10.1128/mcb.6.12.4396. PMC 367222. PMID 3025655.
- ^ Russell RB, Breed J, Barton GJ (June 1992). "Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains". FEBS Letters. 304 (1): 15–20. doi:10.1016/0014-5793(92)80579-6. PMID 1377638. S2CID 7046771.
- ^ Pawson T, Gish GD, Nash P (December 2001). "SH2 domains, interaction modules and cellular wiring". Trends in Cell Biology. 11 (12): 504–511. doi:10.1016/s0962-8924(01)02154-7. PMID 11719057.
- ^ Koytiger G, Kaushansky A, Gordus A, Rush J, Sorger PK, MacBeath G (May 2013). "Phosphotyrosine signaling proteins that drive oncogenesis tend to be highly interconnected". Molecular & Cellular Proteomics. 12 (5): 1204–13. doi:10.1074/mcp.M112.025858. PMC 3650332. PMID 23358503.