Cited by 63Iron Metabolism and DisordersCell Adhesion Molecules ResearchCellular transport and secretion

A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin

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DUBLJEVIC, Valentina, SALI, Adnan, GODING, James W.·1999·Biochemical Journal

Abstract

The transferrin receptor contains a highly conserved Arg-Gly-Asp (RGD) sequence in the C-terminal region where transferrin is thought to bind. RGD sequences are commonly involved in cell adhesion. This sequence is crucial for transferrin binding, suggesting possible evolutionary links between molecules mediating iron uptake and cell adhesion.

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Crossref · 10.1042/bj3410011

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3 of 3 references verified0 citation errors · 0 not checkable

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Authors
DUBLJEVIC, V., SALI, A., & GODING, J. W.
Affiliations
The Alfred Hospital (AU)
Venue
Biochemical Journal
Published
1999-06-24
Volume
341
Issue
1
Pages
11-14
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W1987489188
Cited by
63
References
3
Citations by year
2025: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 3 · 2016: 2 · 2015: 1 · 2013: 4 · 2012: 3
FWCI
2.69
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
transferrin receptor, RGD motif, Arg-Gly-Asp sequence, transferrin binding, iron absorption, cell adhesion, C-terminal region, protein-protein interaction
MeSH terms
Alkaline Phosphatase, Amino Acid Sequence, Humans, Molecular Sequence Data, Oligopeptides, Protein Binding, Receptors, Transferrin, Recombinant Fusion Proteins, Transferrin, Conserved Sequence, Sequence Homology, Amino Acid

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