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The structure and function of HFE
Author(s) -
Drakesmith Hal,
Townsend Alain
Publication year - 2000
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/1521-1878(200007)22:7<595::aid-bies1>3.0.co;2-e
Subject(s) - major histocompatibility complex , transferrin receptor , biology , transferrin , homologous chromosome , function (biology) , genetics , pathogenesis , hemochromatosis , hereditary hemochromatosis , microbiology and biotechnology , receptor , immunology , antigen , biochemistry , gene
The iron overload disease hereditary haemochromatosis (HH) occurs in about 1 in 300 Caucasians; the protein mutated in this disorder is termed HFE.(1) HFE is homologous to major histocompatibility complex (MHC) class I proteins, but unlike MHC class I molecules, HFE does not present peptides to T cells.(2) The transferrin receptor (TfR) is a ligand for HFE, and the crystal structure of the HFE–TfR complex has been determined.(3) The many interesting features of this structure illustrate the diverse roles of the MHC fold in nature and clarify how HFE affects TfR function. Whether the interaction between HFE and TfR explains the pathogenesis of HH is not so clear. BioEssays 22:595–598, 2000. © 2000 John Wiley & Sons, Inc.