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Article

Crystal structure of human thioredoxin revealing an unraveled helix and exposed S-nitrosation site.

Protein science : a publication of the Protein Society - 1 Sept 2010

Weichsel Andrzej, Kem Michelle, Montfort William R

Abstract excerpt

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...

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Identifiers

PMID: 20662007
DOI: 10.1002/pro.455
PMCID: PMC2975143

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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