Structural evidence for adaptive ligand binding of glycolipid transfer protein

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

    Research output: Contribution to journalArticleScientificpeer-review

    41 Citations (Scopus)

    Abstract

    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.
    Original languageUndefined/Unknown
    Pages (from-to)224–236
    Number of pages13
    JournalJournal of Molecular Biology
    Volume355
    Issue number2
    DOIs
    Publication statusPublished - 2006
    MoE publication typeA1 Journal article-refereed

    Keywords

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

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