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

Melanie J. Bennett, José A. Lebrón and Pamela J. Bjorkman ()
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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

Nature, 2000, vol. 403, issue 6765, 46-53

Abstract: 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.

Date: 2000
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DOI: 10.1038/47417

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