User:Brianna Barnes/Sandbox 1

This is a default text for your page Brianna Barnes/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Background

Discovered in 1937 by French scientist Laufberger, ferritin was first detected in horse spleen and a few years later in humans (7). Ferritin is a protein that is responsible for iron storage and iron homeostasis, as well as various physiologic and pathological processes in prokaryotes and eukaryotes. Iron homeostasis is essential to maintaining life because iron can be toxic to DNA and proteins if not properly regulated. If there is an overload of iron, reactive oxygen species can be produced, lipid peroxidation can occur, and there can be damage to DNA. Typically, ferritin presents as a cytosolic protein, but there are also mitochondrial and nuclear forms that have recently been discovered. The most common measurement of ferritin is collected from serum ferritin, which is ferritin stored in red blood cells. Many variations of ferritin exist, as it is presumed that evolutionary adaptations were made in order to allow certain organisms to survive.

Structure

The structure of ferritin consists of a spherical apoferritin shell that has 24 subunits to form a cage that contains two types of subunits: H and L. The ratio of H to L subunits is dependent upon inflammation and tissue type, and varies greatly. H-subunits are mostly found in the kidneys and heart while the L-subunits are mostly found in the liver and spleen. The genes that encode for these H and L subunits are found on chromosomes 11q and 19q (7). Each subunit is constructed from four α-helices, A, B, C, and D, which combine to form helix E. This can be seen in the tertiary structure of ferritin. In the quaternary structure, eukaryotic ferritin presents as spherical with 4-3-2 symmetry. Within the apoferritin shell is where sequestered iron is kept. It contains insoluble iron (III) oxide hydroxide and iron (III) phosphate. Ferritin is able to be degraded through lysosomal or proteasomal mechanisms depending on if degradation is needed.

Function

Bacterioferritin

Clinical Uses

Relevance to Disease/Illness

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.