Ferritin
From Proteopedia
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Contents |
Function
Ferritin (FR) is an iron storage and release protein. It stores iron as microcrystals with phosphate and hydroxide ions. FR is composed of 24 subunits of heavy chain (FTH) a[1]
nd light chain (FTL). Amphibians have an additional middle subunit FR (FTM).
- Bacterioferritin (BFR) structure is very similar to FR. It contains a binuclear iron center and haem. It stores iron as ferric oxide mineral in its hollow central cavity.
- Thioferritin (TFR) is a ferritin-related protein with 2 cysteine residues adjacent to the dimetal binding site.
- Another iron storing protein is the DNA-binding Protein of Starved cells (Dps) - a ferritin-like diiron carboxylate.
- MrgA – another iron storage protein - belongs to the Dps family.
Relevance
Cavities formed by FR are used for the manufacture of nanoparticles. FR is used as a marker for iron overload disorder.
Disease
FR deficiency can lead to anemia.
3D Structures of Ferritin
Updated on 21-January-2016
References
- ↑ Wang W, Knovich MA, Coffman LG, Torti FM, Torti SV. Serum ferritin: Past, present and future. Biochim Biophys Acta. 2010 Aug;1800(8):760-9. doi: 10.1016/j.bbagen.2010.03.011. , Epub 2010 Mar 19. PMID:20304033 doi:http://dx.doi.org/10.1016/j.bbagen.2010.03.011
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Michal Harel, Joel L. Sussman, David Canner, Eran Hodis, Alexander Berchansky

