User:Arthur Migliatti/Sandbox1
From Proteopedia
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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. | ||
| - | '''Thioredoxin'''(Trx) is a protein present in all organisms, from bacterias to complex beings as humans. It has an active site composed of 2 cysteines separated by 2 aminoacids(Cys32 - X - X - Cys35). Trx 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>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. | + | '''Thioredoxin'''(Trx) is a protein present in all organisms, from bacterias to complex beings as humans. It has an active site composed of 2 cysteines separated by 2 aminoacids(Cys32 - X - X - Cys35). Trx 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 14:00, 18 May 2022
Introduction
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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.
