User:Arthur Migliatti/Sandbox1

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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.
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'''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 is It has an active site composed of 2 cysteines separated by 2 aminoacids(Cys32 - X - X - Cys35), and a great amount of functions were interacts with a diverse pool of proteins, acting, when reduced, as a donator of a pair of electrons, and becomes oxidized, being reduced back by '''[[Thioredoxin Reductase]]'''(TrxR), which is reduced in the end by '''NADPH''' <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<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> in a study realized in bacteria, and were described as necessary proteins to reduce '''[[Ribonucleotide Reductase]]'''(RNR), an enzyme involved in DNA replication and repair.
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'''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(Cys32 - X - X - Cys35) 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.
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and a great amount of functions were interacts with a diverse pool of proteins, acting, when reduced, as a donator of a pair of electrons, and becomes oxidized, being reduced back by '''[[Thioredoxin Reductase]]'''(TrxR), which is reduced in the end by '''NADPH''' <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<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> in a study realized in bacteria, and were described as necessary proteins to reduce '''[[Ribonucleotide Reductase]]'''(RNR), an enzyme involved in DNA replication and repair.
Cytosolic, nuclear, mithocondrial and secreted. Fazer distinção antes sobre a Trx1 e a Trx2. Não sei se a Trx2 também possui sítio ativo nesse lugar.
Cytosolic, nuclear, mithocondrial and secreted. Fazer distinção antes sobre a Trx1 e a Trx2. Não sei se a Trx2 também possui sítio ativo nesse lugar.

Revision as of 14:24, 18 May 2022

Introduction

Caption for this structure

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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.

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Arthur Migliatti

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