Zhou MM, Ravichandran KS, Olejniczak EF, Petros AM, Meadows RP, Sattler M, Harlan JE, Wade WS, Burakoff SJ, Fesik SW
Nature. 1995 378 (6557)
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.
MeSH Terms (24)Adaptor Proteins, Signal Transducing Adaptor Proteins, Vesicular Transport Amino Acid Sequence Binding Sites Blood Proteins Ligands Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Peptide Fragments Phospholipids Phosphopeptides Phosphoproteins Phosphotyrosine Protein Conformation Proteins Protein Structure, Secondary Proto-Oncogene Proteins Receptor, trkA Receptor Protein-Tyrosine Kinases Receptors, Nerve Growth Factor Shc Signaling Adaptor Proteins Signal Transduction src Homology Domains