Cited by 315Iron Metabolism and DisordersEnzyme Structure and FunctionCellular transport and secretion

Crystal Structure of the Ectodomain of Human Transferrin Receptor

Lawrence, C. Martin, Ray, Sanjoy, Babyonyshev, Marina, Galluser, Renate, Borhani, David W., Harrison, Stephen C.·1999·Science

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.

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Crossref · 10.1126/science.286.5440.779

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38 of 38 references verified0 citation errors · 0 not checkable

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Authors
Lawrence, C. M., Ray, S., Babyonyshev, M., Galluser, R., Borhani, D. W., & Harrison, S. C.
Affiliations
Howard Hughes Medical Institute (US)
Corresponding author
  • Ray, Sanjoy
  • Borhani, David W.
  • Harrison, Stephen C.
Venue
Science
Published
1999-10-22
Volume
286
Issue
5440
Pages
779-782
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2167563458
Cited by
315
References
38
Citations by year
2026: 6 · 2025: 9 · 2024: 13 · 2023: 13 · 2022: 10 · 2021: 4 · 2020: 15 · 2019: 14 · 2018: 9 · 2017: 5 · 2016: 7 · 2015: 5 · 2014: 7 · 2013: 5 · 2012: 11
FWCI
7.86
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
transferrin receptor, extracellular domain, crystal structure, clathrin-mediated endocytosis, transferrin binding, iron imports, receptor dimer
MeSH terms
Amino Acid Sequence, Animals, Carboxypeptidases, Cell Membrane, Ferric Compounds, Glycosylation, Cricetinae, Humans, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Conformation, Receptors, Transferrin, Transferrin, CHO Cells, Conserved Sequence, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Dimerization

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