BIROn - Birkbeck Institutional Research Online

    The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A

    Tsai, Meng-Lin and Cronin, Nora and Djordjevic, Snezana (2011) The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A. Acta Crystallographica Section D Biological Crystallography 67 (1), pp. 14-24. ISSN 0907-4449.

    Full text not available from this repository.

    Abstract

    Leucine carboxyl methyltransferase 1 (LCMT1) methylates the terminal carboxyl group of the leucine 309 residue of human protein phosphatase 2A (PP2A). PP2A, a key regulator of many cellular processes, has recently generated additional interest as a potential cancer-therapeutic target. The status of PP2A methylation impacts upon the selection of the regulatory subunit by the PP2A core enzyme, thus directing its activity and subcellular localization. An X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 Å. The structure enables the postulation of a mode of interaction with protein phosphatase PP2A and provides a platform for further functional studies of the regulation of methylation of PP2A.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): signal transduction, protein phosphatase 2A, methyltransferases, methylation, protein phosphatase methylesterases
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 14 Feb 2011 14:29
    Last Modified: 11 Oct 2016 12:01
    URI: http://eprints.bbk.ac.uk/id/eprint/3052

    Statistics

    Downloads
    Activity Overview
    0Downloads
    124Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item