English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Human thioredoxin1 (hTRX1) is a small 12-kD oxidoreductase enzyme consisting of 105 amino acids and containing a dithiol/ disulfide active site with multiple cellular functions. This enzyme has activity as a cellular reductase by a dithiol-disulfide exchange reaction using two cysteine residues (Cys32 and Cys35) in the conserved active site sequence. Apart from the two cysteines, there are three additional conserved cysteines, Cys62, Cys69, and Cys73 in the mammalian TRX, which have not been known to their biological functions. Although it has been identified that the Cys73 residue is involved in dimerization of hTRX via an intermolecular disulfide bond formation between Cys73 of each monomer in the oxidized state, biological function of the Cys62 and Cys69 residues in the nonactive remain to be fully elucidated. In the previous paper, researchers proposed that the formation of a disulfide bond between Cys62 and Cys69 could give a way to transiently inhibit hTRX activity for redox signaling or oxidative stress. Furthermore, they proposed a model structure of the non-active site disulfide in the hTRX. Here, we present the high-resolution crystal structure of fully oxidized hTRX1, which shows an intramolecular disulfide bond between Cys62 and Cys69. The disulfide bond formation disengages a helix proximal to the active site and results in a conformational change of the hTRX enzyme, providing a structural basis for understanding the regulation mechanism of redox signaling or oxidative stress.

Joint neutron and X-ray diffraction studies at 293 K of antifreeze protein