Shc, PTB Domain

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.

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