BIROn - Birkbeck Institutional Research Online

    Semisynthetic Src SH2 domains demonstrate altered phosphopeptide specificity induced by incorporation of unnatural lysine derivatives

    Virdee, S. and Macmillan, D. and Waksman, Gabriel (2010) Semisynthetic Src SH2 domains demonstrate altered phosphopeptide specificity induced by incorporation of unnatural lysine derivatives. Chemistry & Biology 17 (3), pp. 274-284. ISSN 1879-1301.

    Full text not available from this repository.

    Abstract

    Site-directed mutagenesis to the 20 natural amino acids becomes a limitation when evaluating subtle perturbations of an amino acid side chain within a protein. To further the study of Src homology 2 (SH2) domain ligand binding, we have developed a system allowing its semisynthesis from three fragments by native chemical ligation. We have replaced a key lysine residue with lysyl derivatives possessing progressively shorter aliphatic side chains. Biophysical characterization of these SH2 domain analogs has allowed for the first time a systematic dissection of the side chain length contribution from a lysine residue to ligand binding. We show that the specificity of the SH2 domain of the Src kinase can be altered by incorporation of such lysyl derivatives, thereby demonstrating the potential of the technique for the development of SH2 domain-based research tools and therapeutics.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): Chembio, signaling, cellbio
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 04 Aug 2010 14:09
    Last Modified: 06 Dec 2016 10:46
    URI: http://eprints.bbk.ac.uk/id/eprint/1178

    Statistics

    Downloads
    Activity Overview
    0Downloads
    87Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item