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Structure and ligand recognition of the phosphotyrosine binding domain of Shc

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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.

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Author notes

  1. Stephen W. Fesik: To whom correspondence should be addressed

Authors and Affiliations

  1. Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois, 60064, USA

    Ming-Ming Zhou, Edward T. Olejniczak, Andrew M. Petros, Robert P. Meadows, Michael Sattler, John E. Harlan, Warren S. Wade & Stephen W. Fesik

  2. Division of Pediatric Oncology, Dana-Farber Cancer Institute,

    Kodimangalam S. Ravichandran & Steven J. Burakoff

  3. Department of Pediatrics, Harvard Medical School, Boston, Massachusetts, 02115, USA

    Kodimangalam S. Ravichandran & Steven J. Burakoff

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  1. Ming-Ming Zhou
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  2. Kodimangalam S. Ravichandran
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  3. Edward T. Olejniczak
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  4. Andrew M. Petros
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  5. Robert P. Meadows
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  6. Michael Sattler
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  7. John E. Harlan
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  8. Warren S. Wade
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  9. Steven J. Burakoff
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Zhou, MM., Ravichandran, K., Olejniczak, E. et al. Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature 378, 584–592 (1995). https://doi.org/10.1038/378584a0

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  • DOI: https://doi.org/10.1038/378584a0

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