Thioredoxin

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[[Image:1ert.png|left|200px|thumb|Crystal Structure of Thioredoxin [[1ert]]]]
 
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{{STRUCTURE_3kd0| PDB=3kd0 | SIZE=400| SCENE= |right|CAPTION=Thioredoxin complex with Cd+2 (yellow) and Cl- (green) ions, [[3kd0]] }}
 
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<StructureSection load='1ert' size='350' side='right' caption='Human thioredoxin (PDB entry [[1ert]])' scene=''>
== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
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The active site motif Cys-Gly-Pro-Cys is involved in the reduction of disulfide bonds in proteins<ref>PMID:8805557</ref>
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</StructureSection>
== 3D Structures of Thioredoxin ==
== 3D Structures of Thioredoxin ==

Revision as of 09:19, 13 September 2016

Human thioredoxin (PDB entry 1ert)

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3D Structures of Thioredoxin

Updated on 13-September-2016

References

  1. ↑ Gleason FK, Holmgren A. Thioredoxin and related proteins in procaryotes. FEMS Microbiol Rev. 1988 Dec;4(4):271-97. PMID:3152490
  2. ↑ Sumida Y, Nakashima T, Yoh T, Furutani M, Hirohama A, Kakisaka Y, Nakajima Y, Ishikawa H, Mitsuyoshi H, Okanoue T, Kashima K, Nakamura H, Yodoi J. Serum thioredoxin levels as a predictor of steatohepatitis in patients with nonalcoholic fatty liver disease. J Hepatol. 2003 Jan;38(1):32-8. PMID:12480557
  3. ↑ Burke-Gaffney A, Callister ME, Nakamura H. Thioredoxin: friend or foe in human disease? Trends Pharmacol Sci. 2005 Aug;26(8):398-404. PMID:15990177 doi:http://dx.doi.org/10.1016/j.tips.2005.06.005
  4. ↑ Weichsel A, Gasdaska JR, Powis G, Montfort WR. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure. 1996 Jun 15;4(6):735-51. PMID:8805557
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