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Structural basis for receptor recognition of vitamin-B12–intrinsic factor complexes

Author

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  • Christian Brix Folsted Andersen

    (Department of Medical Biochemistry,
    Aarhus University, 8000 Aarhus C, Denmark)

  • Mette Madsen

    (Department of Medical Biochemistry,)

  • Tina Storm

    (Department of Medical Biochemistry,)

  • Søren K. Moestrup

    (Department of Medical Biochemistry,)

  • Gregers R. Andersen

    (Aarhus University, 8000 Aarhus C, Denmark)

Abstract

Getting to grips with vitamin B12 Vitamin B12, or cobalamin (Cbl), is an essential coenzyme in mammals that has to be taken up from the diet. Intestinal uptake of the 'extrinsic factor' Cbl is a highly specific process, dependent on gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by cubilin and amnionless. Loss of function of any of these proteins ultimately leads to Cbl deficiency in humans. The crystal structure of the complex between IF–Cbl and the cubilin IF–Cbl-binding region (CUB5–8) has now been determined at 3.3 Å resolution. The structure illuminates how multiple CUB domains collectively function as modular ligand-binding regions, and how two distant CUB domains bind the two IF domains in a Ca2+-dependent fashion.

Suggested Citation

  • Christian Brix Folsted Andersen & Mette Madsen & Tina Storm & Søren K. Moestrup & Gregers R. Andersen, 2010. "Structural basis for receptor recognition of vitamin-B12–intrinsic factor complexes," Nature, Nature, vol. 464(7287), pages 445-448, March.
    • Handle: RePEc:nat:nature:v:464:y:2010:i:7287:d:10.1038_nature08874
    DOI: 10.1038/nature08874
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    Cited by:

    1. Anders Etzerodt & Jakob Hauge Mikkelsen & Morten Torvund-Jensen & Dorle Hennig & Thomas Boesen & Jonas Heilskov Graversen & Søren Kragh Moestrup & Justin M. Kollman & Christian Brix Folsted Andersen, 2024. "The Cryo-EM structure of human CD163 bound to haptoglobin-hemoglobin reveals molecular mechanisms of hemoglobin scavenging," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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