Structural evidence for adaptive ligand binding of glycolipid transfer protein

Tomi Airenne, H Kidron, Yvonne Nymalm, M Nylund, G West, Peter Mattjus, Tiina Salminen

    Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

    44 Citeringar (Scopus)

    Sammanfattning

    Glycolipids participate in many important cellular processes and they are bound and transferred with high specificity by glycolipid transfer protein (GLTP). We have solved three different X-ray structures of bovine GLTP at 1.4 angstrom, 1.6 angstrom and 1.8 angstrom resolution, all with a bound fatty acid or glycolipid. The 1.4 A structure resembles the recently characterized apo-form of the human GLTP but the other two structures represent an intermediate conformation of the apo-GLTPs and the human lactosylceramide-bound GLTP structure. These novel structures give insight into the mechanism of lipid binding and how GLTP may conformationally adapt to different lipids. Furthermore, based on the structural comparison of the GLTP structures and the three-dimensional models of the related Podospora anserina HET-C2 and Arabidopsis thaliana accelerated cell death protein, ACD11, we give structural explanations for their specific lipid binding properties.
    OriginalspråkOdefinierat/okänt
    Sidor (från-till)224–236
    Antal sidor13
    TidskriftJournal of Molecular Biology
    Volym355
    Utgåva2
    DOI
    StatusPublicerad - 2006
    MoE-publikationstypA1 Tidskriftsartikel-refererad

    Nyckelord

    • cavity
    • conformational change
    • crystal structure
    • fluorescence
    • homology modeling

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