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== Function ==
== Function ==
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The primary function of ferritin is it acts as an iron storage mechanism and is used for iron homeostasis. Another reason for the amount of ferritin in the blood is how it's stored and how well the protein is transcribed. Ferritin is found in both eukaryotes and prokaryotes; nearly all living things produce ferritin within the bloodstream to keep iron. As iron storage is precious to living species, it is vital to conserve the protein. Another function is that it makes iron available for critical cellular processes as it protects lipids, DNA, and other proteins from the toxic effects of iron. Although ferritin is widely known for storing and releasing iron within the bloodstream, it can also keep and release other metal ions. The protein is capable of binding beryllium, zinc, aluminum, and copper. <scene name='88/881545/Polar and Non polar/2'>(4V6B)</scene>
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The primary function of ferritin is it acts as an iron storage mechanism and is used for iron homeostasis. Another reason for the amount of ferritin in the blood is how it's stored and how well the protein is transcribed. Ferritin is found in both eukaryotes and prokaryotes; nearly all living things produce ferritin within the bloodstream to keep iron. As iron storage is precious to living species, it is vital to conserve the protein. Another function is that it makes iron available for critical cellular processes as it protects lipids, DNA, and other proteins from the toxic effects of iron. Although ferritin is widely known for storing and releasing iron within the bloodstream, it can also keep and release other metal ions. The protein is capable of binding beryllium, zinc, aluminum, and copper.
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<ref> <i> Ferritin for the Clinician: Knovich, Mary Ann, Storey, Jonathan A., Coffman, Lan G., and Torti, Suzy V. 2009 May ; 23(3): 95–104.</i> [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717717/pdf/nihms113591.pdf doi: 10.1016/j.blre.2008.08.001]. </ref>
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<ref> <i> Knovich, Mary Ann, Storey, Jonathan A., Coffman, Lan G., and Torti, Suzy V., ''Ferritin for the Clinician'' 2009 May ; 23(3): 95–104.</i> [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717717/pdf/nihms113591.pdf doi: 10.1016/j.blre.2008.08.001]. </ref>
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<ref>Martz, E. Book review of <i>Introduction to protein science—architecture, function, and genomics: Lesk, Arthur M.</i>. <i>Biochem. Mol. Biol. Educ.</i> 33:144-5 (2006). [http://dx.doi.org/10.1002/bmb.2005.494033022442 DOI: 10.1002/bmb.2005.494033022442]</ref>.
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<ref> <i>Torti, Frank M., Torti, Suzy V., ''Regulation of ferritin genes and protein'' </i> (2002) 99: 3505-3516. [http://citeseerx.ist.psu.edu/viewdoc/download?doi=10.1.1.318.9363&rep=rep1&type=pdf DOI: 10.1182/blood.V99.10.3505] </ref>
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<ref> <i>Regulation of ferritin genes and protein: Torti, Frank M., Torti, Suzy V. </i> (2002) 99: 3505-3516. [http://citeseerx.ist.psu.edu/viewdoc/download?doi=10.1.1.318.9363&rep=rep1&type=pdf DOI: 10.1182/blood.V99.10.3505] </ref>
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<ref> <i> ''Tri-iodide derivative of apoferritin'' </i> [https://www.rcsb.org/structure/1GWG DOI: 10.2210/pdb1GWG/pdb]</ref>
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<ref> <i> Tri-iodide derivative of apoferritin </i> [https://www.rcsb.org/structure/1GWG DOI: 10.2210/pdb1GWG/pdb]</ref>
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<ref> <i> Casiday, Rachel and Frey, Regina; ''Iron Use and Storage in the Body: Ferritin and Molecular Representations Iron in Biology: Study of the Iron Content in Ferritin, The Iron-Storage Protein''. </i> [http://www.chemistry.wustl.edu/~edudev/LabTutorials/Ferritin/Ferritin.html] </ref>
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<ref> <i> Iron Use and Storage in the Body: Ferritin and Molecular Representations Iron in Biology: Study of the Iron Content in Ferritin, The Iron-Storage Protein. Casiday, Rachel and Frey, Regina </i> [http://www.chemistry.wustl.edu/~edudev/LabTutorials/Ferritin/Ferritin.html] </ref>
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<ref> <i> Stevens, Ruth; ''Edward Stiefel, chemist who bridged domains, dies at age'' 64</i> [https://www.princeton.edu/news/2006/09/09/edward-stiefel-chemist-who-bridged-domains-dies-age-64] </ref>
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<ref> <i> Edward Stiefel, chemist who bridged domains, dies at age 64 by Stevens, Ruth </i> [https://www.princeton.edu/news/2006/09/09/edward-stiefel-chemist-who-bridged-domains-dies-age-64] </ref>
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<ref> <i> Artymiuk, P.J., Harrison, P.M., ''SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS''
== Disease ==
== Disease ==

Revision as of 01:11, 30 April 2021

Crystal Structure of Human Ferritin

Drag the structure with the mouse to rotate

Ferritin

Function

The primary function of ferritin is it acts as an iron storage mechanism and is used for iron homeostasis. Another reason for the amount of ferritin in the blood is how it's stored and how well the protein is transcribed. Ferritin is found in both eukaryotes and prokaryotes; nearly all living things produce ferritin within the bloodstream to keep iron. As iron storage is precious to living species, it is vital to conserve the protein. Another function is that it makes iron available for critical cellular processes as it protects lipids, DNA, and other proteins from the toxic effects of iron. Although ferritin is widely known for storing and releasing iron within the bloodstream, it can also keep and release other metal ions. The protein is capable of binding beryllium, zinc, aluminum, and copper.

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Owen Wostoupal

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