Crystal structure of the ectodomain of human transferrin receptor.
The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome. The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit. One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure. A model is proposed for Tf binding to the receptor.
Lawrence
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Howard Hughes Medical Institute and Children's Hospital Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.
Ray
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Babyonyshev
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M
Galluser
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Borhani
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Harrison
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D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002268:Carboxypeptidases / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry; D017124:Conserved Sequence; D006224:Cricetinae; D018360:Crystallography, X-Ray; D019281:Dimerization; D005290:Ferric Compounds / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011990:Receptors, Transferrin / Q000737:chemistry* / Q000378:metabolism; D014168:Transferrin / Q000378:metabolism
D005290:Ferric Compounds; D011990:Receptors, Transferrin; D014168:Transferrin; D002268:Carboxypeptidases; C026134:glutamate carboxypeptidase