User:Arthur Migliatti/Sandbox1
From Proteopedia
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<StructureSection load='1trs' size='340' side='right' caption='Human Thioredoxin 1'> | <StructureSection load='1trs' size='340' side='right' caption='Human Thioredoxin 1'> | ||
| - | '''Thioredoxin'''(Trx) is a protein present in all organisms, from bacterias to complex beings as humans. This page will be focused on exploring the characteristics of '''Trx1''', a cytosolic form of Trx present in eukaryotes. Trx1 has an active site composed of 2 cysteines separated by 2 aminoacids (<scene name='91/911850/Trx_cys-active_site/2'>Cys32 - X - X - Cys35</scene>) which catalyses the reduction of other thiol-proteins and becomes oxidized. It is reduced back by '''[[Thioredoxin Reductase]]'''(TrxR), which, in the end, is reduced by '''NADPH'''. Together, the two proteins and NADPH form the system Trx<ref>Lu, J.; Holmgren, A. The Thioredoxin Antioxidant System. Free Radical Biology and Medicine 2014, 66, 75–87. https://doi.org/10.1016/j.freeradbiomed.2013.07.036.</ref>. Trx and TrxR were first discovered in 1964 in a study realized in bacteria, and were described as necessary proteins to reduce '''[[Ribonucleotide Reductase]]'''(RNR), a protein that produces deoxyribonucleotides from ribonucleotides<ref>Laurent, T. C.; Moore, E. C.; Reichard, P. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B. J Biol Chem 1964, 239, 3436–3444.</ref>. Since 1964, functions of Trx1 different than participating in cell division were discovered, as denitrosation, transnitrosation, deglutathionylation, | + | '''Thioredoxin'''(Trx) is a protein present in all organisms, from bacterias to complex beings as humans. This page will be focused on exploring the characteristics of '''Trx1''', a cytosolic form of Trx present in eukaryotes. Trx1 has an active site composed of 2 cysteines separated by 2 aminoacids (<scene name='91/911850/Trx_cys-active_site/2'>Cys32 - X - X - Cys35</scene>) which catalyses the reduction of other thiol-proteins and becomes oxidized. It is reduced back by '''[[Thioredoxin Reductase]]'''(TrxR), which, in the end, is reduced by '''NADPH'''. Together, the two proteins and NADPH form the system Trx<ref>Lu, J.; Holmgren, A. The Thioredoxin Antioxidant System. Free Radical Biology and Medicine 2014, 66, 75–87. https://doi.org/10.1016/j.freeradbiomed.2013.07.036.</ref>. |
| + | Trx and TrxR were first discovered in 1964 in a study realized in bacteria, and were described as necessary proteins to reduce '''[[Ribonucleotide Reductase]]'''(RNR), a protein that produces deoxyribonucleotides from ribonucleotides<ref>Laurent, T. C.; Moore, E. C.; Reichard, P. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B. J Biol Chem 1964, 239, 3436–3444.</ref>. Since 1964, functions of Trx1 different than participating in cell division were discovered, as denitrosation, transnitrosation, deglutathionylation, | ||
To reduce other proteins, first happens an attack from Cys32, creating an intermolecular dissulfide bond, represented <scene name='91/911850/C32_s-s_c206/1'>here</scene> between residue Cys32 from Trx1 and residue Cys206 from '''[[MsrA]]'''. After it, residue Cys35 attacks Cys32, creating a dissulfide bond between the two cysteines in Trx1's catalytic site. This is the <scene name='91/911850/Trx_cys_-_oxidized_-_diss_bond/4'>oxidized form of Trx1</scene>. | To reduce other proteins, first happens an attack from Cys32, creating an intermolecular dissulfide bond, represented <scene name='91/911850/C32_s-s_c206/1'>here</scene> between residue Cys32 from Trx1 and residue Cys206 from '''[[MsrA]]'''. After it, residue Cys35 attacks Cys32, creating a dissulfide bond between the two cysteines in Trx1's catalytic site. This is the <scene name='91/911850/Trx_cys_-_oxidized_-_diss_bond/4'>oxidized form of Trx1</scene>. | ||
Revision as of 21:33, 18 June 2022
Introduction
This is a default text for your page Arthur Migliatti/Sandbox1. 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.
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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
- ↑ Lu, J.; Holmgren, A. The Thioredoxin Antioxidant System. Free Radical Biology and Medicine 2014, 66, 75–87. https://doi.org/10.1016/j.freeradbiomed.2013.07.036.
- ↑ Laurent, T. C.; Moore, E. C.; Reichard, P. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B. J Biol Chem 1964, 239, 3436–3444.
- ↑ Tao, L.; Gao, E.; Bryan, N. S.; Qu, Y.; Liu, H.-R.; Hu, A.; Christopher, T. A.; Lopez, B. L.; Yodoi, J.; Koch, W. J.; Feelisch, M.; Ma, X. L. Cardioprotective Effects of Thioredoxin in Myocardial Ischemia and the Reperfusion Role of S-Nitrosation. Proc Natl Acad Sci U S A 2004, 101 (31), 11471–11476. https://doi.org/10.1073/pnas.0402941101.
- ↑ Tao, L.; Gao, E.; Bryan, N. S.; Qu, Y.; Liu, H.-R.; Hu, A.; Christopher, T. A.; Lopez, B. L.; Yodoi, J.; Koch, W. J.; Feelisch, M.; Ma, X. L. Cardioprotective Effects of Thioredoxin in Myocardial Ischemia and the Reperfusion Role of S-Nitrosation. Proc Natl Acad Sci U S A 2004, 101 (31), 11471–11476. https://doi.org/10.1073/pnas.0402941101.
