The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Crystal Structure of Human Frataxin
Open accessAbstract
Friedreich's ataxia, an autosomal recessive neurodegenerative disorder characterized by progressive gait and limb ataxia, cardiomyopathy, and diabetes mellitus, is caused by decreased frataxin production or function. The structure of human frataxin, which we have determined at 1.8-A resolution, reveals a novel protein fold. A five-stranded, antiparallel beta sheet provides a flat platform, which supports a pair of parallel alpha helices, to form a compact alphabeta sandwich. A cluster of 12 acidic residues from the first helix and the first strand of the large sheet form a contiguous anionic surface on the protein. The overall protein structure and the anionic patch are conserved in eukaryotes, including animals, plants, and yeast, and in prokaryotes. Additional conserved residues create an extended 1008-A(2) patch on a distinct surface of the protein. Side chains of disease-associated mutations either contribute to the anionic patch, help create the second conserved surface, or point toward frataxin's hydrophobic core. These structural findings predict potential modes of protein-protein and protein-iron binding.
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“Exogenous Fpn expressed in Xenopus oocytes served as a ferrous iron exporter (72).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [72]
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“Simultaneous studies characterized Fpn, which is abundantly expressed on the basolateral membrane of polarized enterocytes in the duodenum, in the cytosol of reticuloendothelial cells, and on the basal surface of syncytiotrophoblasts of the placenta (1, 72, 198).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [72]
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“Fpn (also termed Ireg1, MTP1) was originally identified by positional cloning to identify the causative gene for hypochromic anemia of “weissherbst” mutant zebrafish (72).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [72]
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Intracellular iron transport and storage: from molecular mechanisms to health implications
Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526
Frataxin Acts as an Iron Chaperone Protein to Modulate Mitochondrial Aconitase Activity
Bulteau, A.-L., O’Neill, H. A., Kennedy, M. C., Ikeda‐Saito, M., Isaya, G., & Szweda, L. I. (2004) · Science · doi:10.1126/science.1098991 · Cited by 372
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Metadata
- Authors
- Dhe-Paganon, S., Shigeta, R., Chi, Y.-I., Ristow, M., & Shoelson, S. E.
- Affiliations
- Joslin Diabetes Center (US)
- Corresponding author
- Shoelson, Steven E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 275
- Issue
- 40
- Pages
- 30753-30756
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2105822562
- Cited by
- 226
- References
- 32
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 6 · 2023: 6 · 2022: 9 · 2021: 6 · 2020: 10 · 2019: 10 · 2018: 7 · 2017: 8 · 2016: 4 · 2015: 9 · 2014: 10 · 2013: 14 · 2012: 3
- FWCI
- 8.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Joslin Diabetes Center
- Universität zu Köln
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (DK4312, DK07260, T32DK007260)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- frataxin, Friedreich's ataxia, protein crystal structure, novel protein fold, anionic surfaces, disease-associated mutations, protein-protein interaction, hydrophobic core
- MeSH terms
- Frataxin, Amino Acid Sequence, Cloning, Molecular, Friedreich Ataxia, Humans, Iron, Models, Molecular, Molecular Sequence Data, Protein Binding, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Protein Structure, Secondary, Protein Folding, Phosphotransferases (Alcohol Group Acceptor), Crystallography, X-Ray, Iron-Binding Proteins
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