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Nature. 1995 Dec 7;378(6557):584-92.

Structure and ligand recognition of the phosphotyrosine binding domain of Shc.

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  • 1Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064, USA.


The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of Shc complexed to a phosphopeptide reveals an alternative means of recognizing tyrosine-phosphorylated proteins. Unlike in SH2 domains, the phosphopeptide forms an antiparallel beta-strand with a beta-sheet of the protein, interacts with a hydrophobic pocket through the (pY-5) residue, and adopts a beta-turn. The PTB domain is structurally similar to pleckstrin homology domains (a beta-sandwich capped by an alpha-helix) and binds to acidic phospholipids, suggesting a possible role in membrane localization.

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