The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Crystal Structure of the Ectodomain of Human Transferrin Receptor
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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“In this manner, HFE appears to block Tf binding to TfR through direct competition for the same binding site (179).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [179]
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- Letters A to H designate the eight TfR monomers in the crystallographic asymmetric unit. The physiological dimers were identified by the proximity of their NH 2 -termini. They are the four pairs AB CD EF and GH related to each other by the 8 5 noncrystallographic symmetry. Each dimer interface has a large solvent-inaccessible surface area of 4100 Å 2 . There are also significant contacts between successive dimers within the 8 5 helical columns (2600 Å 2 ).
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Metadata
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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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