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Article

Structure of human thioredoxin exhibits a large conformational change.

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

Hall Gareth, Emsley Jonas

Abstract excerpt

Thioredoxin is an oxidoreductase, which is ubiquitously present across phyla from humans to plants and bacteria. Thioredoxin reduces a variety of substrates through active site Cys 32, which is subsequently oxidized to form the intramolecular disulphide with Cys 35. The thioredoxin fold is known to be highly stable and conformational changes in the active site loops and residues Cys 32, Cys 35 have been...

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Identifiers

PMID: 20661909
DOI: 10.1002/pro.466
PMCID: PMC2975144

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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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