Structure and ligand recognition of the phosphotyrosine binding domain of Shc

Ming Ming Zhou, Kodimangalam S. Ravichandran, Edward T. Olejniczak, Andrew M. Petros, Robert P. Meadows, Michael Sattler, John E. Harlan, Warren S. Wade, Steven J. Burakoff, Stephen W. Fesik

Research output: Contribution to journalArticlepeer-review

325 Scopus citations


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.

Original languageEnglish
Pages (from-to)584-592
Number of pages9
Issue number6557
StatePublished - Dec 7 1995


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