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Trx1 is a monomeric protein and weights around 12kDa. It is formed by 4 beta sheets involved by 4 alpha helix, shown <scene name='91/911850/Trx-bsheet-ahelix/1'>here</scene>.
Trx1 is a monomeric protein and weights around 12kDa. It is formed by 4 beta sheets involved by 4 alpha helix, shown <scene name='91/911850/Trx-bsheet-ahelix/1'>here</scene>.
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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,
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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, other functions of Trx1, different than participating in cell division, were discovered, as denitrosation and transnitrosation for example. Denitrosation is the removal of NO of a protein, and Trx1 does it by being temporarily S-nitrosataded on Cys32. Aterwards, Cys35 attacks Cys32 and forms a dissulfide bond, releasing HNO/NO to the medium. On the other hand, transnitrosation is the the form
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 21:57, 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.

Human Thioredoxin 1

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References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.

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