The Shc transforming protein's function isn't fully understood, however, it may link activated growth factor receptors to a signaling pathway which in turn regulates the proliferation of mammalian cells. Also, this protein may play a role in the transformation of oncogenic tyrosine kinases. The SH2 domain shown here resides in the C terminal region of the protein. The SH2 domain, or Src homology-2 domain, are about 100 amino acid residues long and are found in intracellular signal-transduction proteins. This domain recognizes and binds phosphotyrosine-containing sequences with a high specificity in proteins that participate in signaling by growth factors and oncogenes.
The SH2 domain of Shc is 107 amino acid residues long. Its structure consists of 3 alpha-helices (gold) and 5 beta-strands (blue). The phosphopeptide that is shown in complex with the SH2 domain is 14 amino acid residues long and is as follows: Gly-His-Asp-Gly-Leu-pTyr-Gln-Gly-Leu-Ser-Thr-Ala-Thr-Lys.

• Keywords: SH2 Domain, Complex (Signal Transduction/Peptide)
• View this protein's PDB entry as 1TCE
• References:
  • M.M. Zhou, R.P. Meadows, T.M. Logan, H.S. Yoon, W.S. Wade, K.S. Ravichandran, S.J. Burakoff, S.W. Fesik
    Solution Structure of the Shc SH2 Domain Complexed With a Tyrosine-Phosphorylated Peptide From the T-Cell Receptor.
    Proc. Nat. Acad. Sci. USA 92:7784 (1995)
    
  • S.M. Pascal, A.U. Singer, G. Gish, T. Yamazaki, S.E. Shoelson, T. Pawson, L.E. Kay, J.D. Forman-Kay
    Nuclear Magnetic Resonance Structure of an SH2 Domain of Phospholipase C-Gamma 1 Complexed With a High Affinity Binding Peptide.
    Cell 77:461 (1994)
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  • G. Waksman, S.E. Shoelson, N. Pant, D. Cowburn, J. Kuriyan
    Binding of a High Affinity Phosphotyrosyl Peptide to the Src SH2 Domain: Crystal Structures of the Complexed and Peptide-free Forms.
    Cell 72:779 (1993)
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  • M.J. Eck, S.E. Shoelson, S.C. Harrison
    Recognition of a High-Affinity Phophotyrosyl Peptide by the Src Homology-2 Domain of P56lck.
    Nature 362:87 (1993)
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