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    Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

    Waksman, Gabriel and Kominos, D. and Robertson, S. and Pant, N. and Baltimore, R. and Birge, D. and Cowburn, H. and Hanafusa, B. and Mayer, B. and Overduin, M. and Resh, M. and Rios, C. and Silverman, L. and Kuriyan, J. (1992) Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature 358 , pp. 646-653. ISSN 0028-0836.

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    Abstract

    Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 Å, respectively. A central antiparallel β-sheet in the structure is flanked by two α-helices, with peptide binding mediated by the sheet, intervening loops and one of the helices. The specific recognition of phosphotyrosine involves amino–aromatic interactions between lysine and arginine side chains and the ring system in addition to hydrogen-bonding interactions with the phosphate.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 29 Apr 2019 16:01
    Last Modified: 29 Apr 2019 16:01
    URI: http://eprints.bbk.ac.uk/id/eprint/27353

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