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Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor

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An Addendum to this article was published on 12 April 2007

Abstract

The crystal structure of the tandem SH2 domains of human ZAP-70 in complex with a peptide derived from the ζ-subunit of the T-cell receptor reveals an unanticipated interaction between the two domains. A coiled coil of α-helices connects the two SH2 domains, producing an interface that constitutes one of the two critical phosphotyrosine binding sites. These and other unique features provide the molecular basis for highly selective association of ZAP-70 with the T-cell receptor.

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Author notes

  1. Jay P. Morgenstern & Kelly Theriault

    Present address: Millenium Pharmaceuticals, 41 second St., Cambridge, MA, 02141, USA

  2. Meizhen Lou

    Present address: , 1 Kingsvilla St, Footscary West, Victoria, 3012, Australia

  3. Chris S. Marr

    Present address: Chemistry Dept, Tuffs University, Malden, MA, 02148, USA

Authors and Affiliations

  1. ARIAD Pharmaceutical, Inc., 26 Landsdowne Street, Cambridge, Massachusetts, 02139-4234, USA

    Marcos H. Hatada, Xiaode Lu, Ellen R. Laird, Jeremy Green, Jay P. Morgenstern, Meizhen Lou, Chris S. Marr, Thomas B. Phillips, Mary K. Ram, Kelly Theriault, Mark J. Zoller & Jennifer L. Karas

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  1. Marcos H. Hatada
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  2. Xiaode Lu
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Hatada, M., Lu, X., Laird, E. et al. Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor. Nature 377, 32–38 (1995). https://doi.org/10.1038/377032a0

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  • DOI: https://doi.org/10.1038/377032a0

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