Sandbox Reserved 186
From Proteopedia
(Undo revision 1918887 by Drew Barber (Talk)) |
(Undo revision 1918887 by Drew Barber (Talk)) |
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{{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_Drew_Barber}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Your Heading Here (maybe something like 'Structure')== | ==Your Heading Here (maybe something like 'Structure')== | ||
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. 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 <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
Revision as of 02:46, 30 April 2014
| This Sandbox is Reserved from 4/28/214, through 6/28/214 for use in the course "Proteins" taught by Drew Barber at the Univeristy of Vermont. This reservation includes Sandbox Reserved 186 through Sandbox Reserved 189. |
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Contents |
Your Heading Here (maybe something like 'Structure')
This is a default text for your page '. 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.
Overview
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).
Secondary Structure and the Thioredoxin Like Fold
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form. Interestingly two of the β-strands form a parallel β-sheet. Overall GPx-1 exhibits a thioredoxin like fold (Figure 2). The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).
Relevance
Structural highlights
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.
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
