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Showing 1–4 of 4 results
Advanced filters: Author: Remy Sounier Clear advanced filters
  • Alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. Here authors solve the Xray structure of human ACER3 and uncover a Ca2+ binding site providing an explanation for the known regulatory role of Ca2+ on ACER3 activity.

    • Ieva Vasiliauskaité-Brooks
    • Robert D. Healey
    • Sébastien Granier
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-13
  • Structures of the adiponectin receptors ADIPOR1 and ADIPOR2 combined with molecular dynamics simulations and enzymatic assays suggest that both receptors have intrinsic ceramidase activity.

    • Ieva Vasiliauskaité-Brooks
    • Remy Sounier
    • Sébastien Granier
    Research
    Nature
    Volume: 544, P: 120-123
  • NMR structure determination is challenging for proteins with a molecular weight above 30 kDa and atomic-resolution structure determination from cryo-EM data is currently not the rule. Here the authors describe an integrated structure determination approach that simultaneously uses NMR and EM data and allows them to determine the structure of the 468 kDa dodecameric aminopeptidase TET2 complex.

    • Diego F. Gauto
    • Leandro F. Estrozi
    • Jerome Boisbouvier
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12
  • NMR spectroscopy reveals the conformational changes of the μ-opioid receptor that are associated with receptor activation, helping to explain why the allosteric coupling between the agonist-binding pocket and the cytoplasmic G-protein-coupling interface of this receptor is relatively weak.

    • Rémy Sounier
    • Camille Mas
    • Sébastien Granier
    Research
    Nature
    Volume: 524, P: 375-378