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Structure and ligand recognition of the phosphotyrosine binding domain of Shc. 1995
M M Zhou, and
K S Ravichandran, and
E F Olejniczak, and
A M Petros, and
R P Meadows, and
M Sattler, and
J E Harlan, and
W S Wade, and
S J Burakoff, and
S W Fesik
Pharmaceutical 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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