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Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor

Author

Listed:
  • Melanie J. Bennett

    (Division of Biology 156-29)

  • José A. Lebrón

    (Division of Biology 156-29)

  • Pamela J. Bjorkman

    (Howard Hughes Medical Institute, California Institute of Technology)

Abstract

HFE is related to major histocompatibility complex (MHC) class I proteins and is mutated in the iron-overload disease hereditary haemochromatosis. HFE binds to the transferrin receptor (TfR), a receptor by which cells acquire iron-loaded transferrin. The 2.8 Å crystal structure of a complex between the extracellular portions of HFE and TfR shows two HFE molecules which grasp each side of a twofold symmetric TfR dimer. On a cell membrane containing both proteins, HFE would ‘lie down’ parallel to the membrane, such that the HFE helices that delineate the counterpart of the MHC peptide-binding groove make extensive contacts with helices in the TfR dimerization domain. The structures of TfR alone and complexed with HFE differ in their domain arrangement and dimer interfaces, providing a mechanism for communicating binding events between TfR chains. The HFE–TfR complex suggests a binding site for transferrin on TfR and sheds light upon the function of HFE in regulating iron homeostasis.

Suggested Citation

  • Melanie J. Bennett & José A. Lebrón & Pamela J. Bjorkman, 2000. "Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor," Nature, Nature, vol. 403(6765), pages 46-53, January.
    • Handle: RePEc:nat:nature:v:403:y:2000:i:6765:d:10.1038_47417
    DOI: 10.1038/47417
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