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

Article Details

Citation

Zhou MM, Ravichandran KS, Olejniczak EF, Petros AM, Meadows RP, Sattler M, Harlan JE, Wade WS, Burakoff SJ, Fesik SW

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

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

PubMed ID
8524391 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
High affinity nerve growth factor receptorP04629Details