Structure and ligand recognition of the phosphotyrosine binding domain of Shc
- 1 December 1995
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 378 (6557), 584-592
- https://doi.org/10.1038/378584a0
Abstract
The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of She complexed to a phosphopeptide reveals an alternative means of recognizing tryosine-phosphorylated proteins. Unlike in SH2 domains, the phosphopeptide forms an antiparallel β-strand with a β-sheet of the protein, interacts with a hydrophobic pocket through the (pY–5) residue, and adopts a β-turn. The PTB domain is structurally similar to pleckstrin homology domains (a β-sandwich capped by an α-helix) and binds to acidic phospholipids, suggesting a possible role in membrane localization.Keywords
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