Shc is a protein that is thought to play a role in signal transduction. It may link activated growth factor receptors to a signaling pathway which regulates the proliferation of mammalian cells as well as play a role in the transformation of oncogenic tyrosine kinases. The phosphotyrosine binding (PTB) domain of Shc is shown here. Like the SH2 domain of Shc, this domain binds tyrosine-phosphorylated proteins as well.
The PTB domain of Shc is 195 amino acid residues long. It consists of 3 alpha-helices (pink) and 7 beta-sheets (blue). Structurally, it is similar to the pleckstrin homology domain in which a beta-sandwich is capped by an alpha-helix. Also, the PTB domain binds to acidic phospholipids which may imply a role in membrane localization. The protein is shown bound to a 12 amino acid residue long phosphopeptide, and the sequence is as follows: His-Ile-Ile-Glu-Asn-Pro-Gln-pTyr-Phe-Ser-Asp-Ala.

• Keywords: Complex (Signal Transduction/Peptide), Phosphotyrosine Binding Domain (PTB).
  
• View this protein's PDB entry as 1SHC
• References:
  • M.M. Zhou, K.S. Ravichandran, E.F. Olejniczak, A.M. Petros, R.P. Meadows, M. Sattler, J.E. Harlan, W.S. Wade, J. Burakoff, S.W. Fesik
    Structure and Ligand Recognition of the Phosphotyrosine Binding Domain of Shc.
    Nature 378:584 (1995)
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  • M.M. Zhou, B. Huang, E.T. Olejniczak, R.P. Meadows, S.B. Shuker, M. Miyazaki, T. Trub, S.E. Shoelson, S.W. Fesik
    Structural Basis For IL-4 Receptor Phosphopeptide Recognition by the IRS-1 PTB Domain.
    Nat. Struct. Biol. 3:388 (1996)
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  • T. Trub, W.E. Choi, G. Wolf, E. Ottinger, Y. Chen, M. Weiss, S.E. Shoelson
    Specificity of the PTB Domain of Shc For Beta Turn-Forming Pentapeptide Motifs Amino-Terminal to Phosphotyrosine.
    J. Biol. Chem. 270:18205 (1995)
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  • W.M. Kavanaugh, L.T. Williams
    An Alternative to SH2 Domains For Binding Tyrosine-Phosphorylated Proteins.
    Science 266:1862 (1994)
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