1DE4

HEMOCHROMATOSIS PROTEIN HFE COMPLEXED WITH TRANSFERRIN RECEPTOR

Summary for 1DE4

• Entry DOI: 10.2210/pdb1de4/pdb
• Related: 1A6Z 1CX8
• Descriptor: HEMOCHROMATOSIS PROTEIN, BETA-2-MICROGLOBULIN, TRANSFERRIN RECEPTOR, ... (7 entities in total)
• Functional Keywords: hfe, hereditary hemochromatosis, mhc class i, transferrin receptor, metal transport inhibitor-receptor complex, metal transport inhibitor/receptor
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 9
• Total formula weight: 348560.51

Authors

Bennett, M.J.,Lebron, J.A.,Bjorkman, P.J. (deposition date: 1999-11-12, release date: 2000-01-19, Last modification date: 2020-07-29)

Primary citation

Bennett, M.J.,Lebron, J.A.,Bjorkman, P.J.
Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor.
Nature, 403:46-53, 2000

PubMed 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 A 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.

PubMed: 10638746
DOI: 10.1038/47417

Experimental method

X-RAY DIFFRACTION (2.8 Å)