BIROn - Birkbeck Institutional Research Online

    Binding of a high affinity phosphotyrosyl peptide to the src SH2 domain: crystal structures of the complexed and peptide-free forms

    Waksman, Gabriel and Shoelson, S. and Pant, N. and Cowburn, D. and Kuriyan, J. (1993) Binding of a high affinity phosphotyrosyl peptide to the src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72 (5), pp. 779-790. ISSN 0092-8674.

    Full text not available from this repository.

    Abstract

    The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide has been determined at 2.7 Å resolution by X-ray diffraction. The peptide binds in an extended conformation and makes primary interactions with the SH2 domain at six central residues: PQ(pY)EEI. The phosphotyrosine and the isoleucine are tightly bound by two well-defined pockets on the protein surface, resulting in a complex that resembles a two-pronged plug engaging a two-holed socket. The glutamate residues are in solvent-exposed environments in the vicinity of basic side chains of the SH2 domain, and the two N-terminal residues cap the phosphotyrosine-binding site. The crystal structure of Src SH2 in the absence of peptide has been determined at 2.5 Å resolution, and comparison with the structure of the high affinity complex reveals only localized and relatively small changes.

    Metadata

    Item Type: Article
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Depositing User: Sarah Hall
    Date Deposited: 29 Apr 2019 15:52
    Last Modified: 02 Aug 2023 17:51
    URI: https://eprints.bbk.ac.uk/id/eprint/27352

    Statistics

    Activity Overview
    6 month trend
    0Downloads
    6 month trend
    369Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item
    Edit/View Item