Sandbox Reserved 978
From Proteopedia
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The catalytic site for TrxR is a -Cys-Val-Asn-Val-Gly-Cys- group that is located by the FAD site allowing for the easy transport of the extra electrons to the Thioredoxin present. | The catalytic site for TrxR is a -Cys-Val-Asn-Val-Gly-Cys- group that is located by the FAD site allowing for the easy transport of the extra electrons to the Thioredoxin present. | ||
| - | A second function of this protein is utilized in the regulation of DNA translation and in apoptosis. A normal stop codon (UGA, UAA, and UAG) stops the translation of the mRNA, but in the presence of TrxR an extra Selenocysteine is added to the end of the protein chain. This extra amino acid is what marks the structure for death inside the cell. Enough of these structures in the cell and the entire cell will undergo apoptosis. | + | A second function of this protein is utilized in the regulation of DNA translation and in apoptosis. A normal stop codon (UGA, UAA, and UAG) stops the translation of the mRNA, but in the presence of TrxR an extra Selenocysteine is added to the end of the protein chain. This extra amino acid is what marks the structure for death inside the cell. Enough of these structures in the cell and the entire cell will undergo apoptosis. |
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== Disease == | == Disease == | ||
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There needs to be be great surveillance on TrxR. Since the enzyme's action works specifically with cell death it needs to be highly regulated. Leaving TrxR unchecked could lead to too little or too much cell death. If TrxR is mutated or inhibited apoptosis is avoided tumors can form | There needs to be be great surveillance on TrxR. Since the enzyme's action works specifically with cell death it needs to be highly regulated. Leaving TrxR unchecked could lead to too little or too much cell death. If TrxR is mutated or inhibited apoptosis is avoided tumors can form | ||
== Structural highlights == | == Structural highlights == | ||
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| + | -Cys-Gly-Pro-Cys- End of Beta-2 strand before alpha-helix | ||
| + | The Cys link in a disulphide and then nearby His causes breaking of disulphide bond in thioredoxin | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Revision as of 03:45, 1 May 2015
| This Sandbox is Reserved from 15-Jan-2015, through 30-May-2015 for use in the course "Biochemistry" taught by Jason Telford at the Maryville University. This reservation includes Sandbox Reserved 977 through Sandbox Reserved 986. |
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Thioredoxin Reductase
Thioredoxin Reductase (TrxR) is a protein in the family of flavoproteins and whose function is very similar to proteins such as glutathione reductase. These types of proteins have two locations other than the active site for bot FAD and NADPH to bind, with the active site being the location of a oxidation/reduction reaction. This redox reaction targets the disulphide group of Thioredoxin in the active site. With the structure of TrxR varying slightly between the likes of bacteria, archaea, and other animals, the action of the family of TrxR remain the same. TrxR is utilized in the regulation of DNA translation and in apoptosis. Each member of the TrxR family has a different way to program the cell for death. These methods range from marking a protein with an extra amino acid to the reduction of H2O2 and even including protein repair.
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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
