Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2

Mari Lehtimäki, Saara Laulumaa, Salla Ruskamo, Petri Kursula

    9 Citationer (Scopus)

    Abstract

    The myelin sheath is a multilayered membrane that surrounds and insulates axons in the nervous system. One of the proteins specific to the peripheral nerve myelin is P2, a protein that is able to stack lipid bilayers. With the goal of obtaining detailed information on the structure-function relationship of P2, 14 structure-based mutated variants of human P2 were generated and produced. The mutants were designed to potentially affect the binding of lipid bilayers by P2. All mutated variants were also crystallized and preliminary crystallographic data are presented. The structural data from the mutants will be combined with diverse functional assays in order to elucidate the fine details of P2 function at the molecular level.

    OriginalsprogEngelsk
    TidsskriftActa Crystallographica Section F: Structural Biology Communications
    Vol/bind68
    Udgave nummerPt 11
    Sider (fra-til)1359-62
    Antal sider4
    ISSN2053-230X
    DOI
    StatusUdgivet - 1 nov. 2012

    Fingeraftryk

    Dyk ned i forskningsemnerne om 'Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2'. Sammen danner de et unikt fingeraftryk.

    Citationsformater