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PMID: 10531064 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Crystal structure of the ectodomain of human transferrin receptor.

Science (New York, N.Y.) ·Vol. 286 ·No. 5440 ·1999-10-22 ·Pages 779-82

Lawrence CM, Ray S, Babyonyshev M, Galluser R, Borhani DW, Harrison SC

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals CHO Cells Carboxypeptidases/chemistry Cell Membrane/chemistry Conserved Sequence Cricetinae Crystallography, X-Ray Dimerization Ferric Compounds/metabolism Glycosylation Humans Hydrogen-Ion Concentration Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Receptors, Transferrin/chemistry,metabolism Transferrin/metabolism
Chemicals
Ferric Compounds Receptors, Transferrin Transferrin Carboxypeptidases glutamate carboxypeptidase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Lawrence C M
Howard Hughes Medical Institute and Children's Hospital Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.
Ray S
Babyonyshev M
Galluser R
Borhani D W
Harrison S C
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
DOI
10.1126/science.286.5440.779
Published
1999-10-22
Pages
779-82
Language
English
Region
United States
NLM ID
0404511
Subset
IM
External Links
PubMed source DOI: 10.1126/science.286.5440.779 View journal details
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