ArticleProtein science : a publication of the Protein Society2010
Crystal structure of human thioredoxin revealing an unraveled helix and exposed S-nitrosation site.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Deciphering the Path ofAntioxidants (Basel, Switzerland) · 2022Article
- Modulation of signaling mechanisms in the heart by thioredoxin 1.Free radical biology & medicine · 2017Review
- Binding of phenothiazines into allosteric hydrophobic pocket of human thioredoxin 1.European biophysics journal : EBJ · 2016Article
- Structures of the reduced and oxidized state of the mutant D24A of yeast thioredoxin 1: insights into the mechanism for the closing of the water cavity.Journal of biomolecular NMR · 2015Article
- Contribution of Fdh3 and Glr1 to Glutathione Redox State, Stress Adaptation and Virulence in Candida albicans.PloS one · 2015Article
- Crystallographic studies evidencing the high energy tolerance to disrupting the interface disulfide bond of thioredoxin 1 from white leg shrimp Litopenaeus vannamei.Molecules (Basel, Switzerland) · 2014Article
- Protective effect of placenta extracts against nitrite-induced oxidative stress in human erythrocytes.Cellular & molecular biology letters · 2012Article
- Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase.Chemical reviews · 2011Review
- Site-specific and redox-controlled S-nitrosation of thioredoxin.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Thioredoxins reduce disulfide bonds and other thiol modifications in all cells using a CXXC motif. Human thioredoxin 1 is unusual in that it codes for an additional three cysteines in its 105 amino acid sequence, each of which have been implicated in other reductive activities. Cys 62 and Cys 69 are buried in the protein interior and lie at either end of a short helix (helix 3), and yet can disulfide link under oxidizing conditions. Cys 62 is readily S-nitrosated, giving rise to a SNO modification, which is also buried. Here, we present two crystal structures of the C69S/C73S mutant protein under oxidizing (1.5 A) and reducing (1.1 A) conditions. In the oxidized structure, helix 3 is unraveled and displays a new conformation that is stabilized by a series of new hydrogen bonds and a disulfide link with Cys 62 in a neighboring molecule. The new conformation provides an explanation for how a completely buried residue can participate in SNO exchange reactions.
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