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Showing 1–3 of 3 results
Advanced filters: Author: Morten Torvund-Jensen Clear advanced filters

  • This study reports the crystal structure of porcine haptoglobin in complex with haemoglobin at 2.9 Å resolution; this provides a structural basis of haptoglobin-mediated recognition of haemoglobin, and insight into the protective role of haptoglobin at the atomic level.

    • Christian Brix Folsted Andersen
    • Morten Torvund-Jensen
    • Søren Kragh Moestrup
    Research
    Nature
    Volume: 489, P: 456-459

  • CD163, a macrophage receptor, is essential for clearing hemoglobin during hemolysis to prevent oxidative damage. Here, the authors reveal the cryo-electron microscopy structure of CD163 bound to haptoglobin-hemoglobin, uncovering calcium-dependent interactions critical for its function and oligomerization.

    • Anders Etzerodt
    • Jakob Hauge Mikkelsen
    • Christian Brix Folsted Andersen
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13

  • Trypanosomes, responsible for sleeping sickness, acquire haem through binding haptoglobin(Hp)–haemoglobin(Hb) complexes in human blood. Here Stødkilde et al. determine the structure of human Hp–Hb in complex with the Hp–Hb receptor from T. bruceiand show that the recognition elements are shared by a protein complex on the surface of a trypanolytic lipoprotein particle.

    • Kristian Stødkilde
    • Morten Torvund-Jensen
    • Christian B. F. Andersen
    Research
    Nature Communications
    Volume: 5, P: 1-8