User:Arthur Migliatti/Sandbox1

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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, 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
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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>.
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>.
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Although Trx1 from a great amount of organisms has only the catalytic site cysteines, the human form of Trx1 also has other <scene name='91/911850/Structural_cysteines/3'>3 structural cysteines</scene>, Cys 62, Cys 69 and Cys 73, which can act as regulators of the protein. <scene name='91/911850/Snocys69/2'>S-nitrosation of Trx on Cys69</scene> enhances its antiapoptotic function in some cases, although its not necessary for it.<ref>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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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 nitrosation of other proteins, that the Trx1 of some species can do.
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</ref>
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Although Trx1 from a great amount of organisms has only the catalytic site cysteines, the human form of Trx1 also has other <scene name='91/911850/Structural_cysteines/3'>3 structural cysteines</scene>, Cys 62, Cys 69 and Cys 73, which can act as regulators of the protein. <scene name='91/911850/Snocys69/2'>S-nitrosation of Trx on Cys69</scene> enhances its antiapoptotic function in some cases, although its not necessary for it.<ref>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.</ref>. Cys 73 has more than one function. Firstly, it is through this residue that Trx1 transnitrosate other proteins, the Trx of not all organisms are capable of doing transnitrosation. Other function is to make Trx1 a sensor of the redox state of the cell.

Revision as of 22:50, 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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