Ontology highlight
ABSTRACT:
SUBMITTER: Marchand CH
PROVIDER: S-EPMC6356897 | biostudies-literature | 2019 Jan
REPOSITORIES: biostudies-literature
Marchand Christophe H CH Fermani Simona S Rossi Jacopo J Gurrieri Libero L Tedesco Daniele D Henri Julien J Sparla Francesca F Trost Paolo P Lemaire Stéphane D SD Zaffagnini Mirko M
Antioxidants (Basel, Switzerland) 20190101 1
Thioredoxins (TRXs) are major protein disulfide reductases of the cell. Their redox activity relies on a conserved Trp-Cys-(Gly/Pro)-Pro-Cys active site bearing two cysteine (Cys) residues that can be found either as free thiols (reduced TRXs) or linked together by a disulfide bond (oxidized TRXs) during the catalytic cycle. Their reactivity is crucial for TRX activity, and depends on the active site microenvironment. Here, we solved and compared the 3D structure of reduced and oxidized TRX h1 f ...[more]