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1.8.1.B1: thioredoxin glutathione reductase

This is an abbreviated version!
For detailed information about thioredoxin glutathione reductase, go to the full flat file.

Word Map on EC 1.8.1.B1

Reaction

glutathione disulfide
+
NADPH
 +
H+
= 2 glutathione +
NADP+

Synonyms

cTGR, DmTrxR, EgTGR, mTGR, SmTGR, TGR, TGRsec, thioredoxin glutathione reductase, thioredoxin-glutathione reductase, thioredoxin/glutathione reductase

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.B1 thioredoxin glutathione reductase

Crystallization

Crystallization on EC 1.8.1.B1 - thioredoxin glutathione reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.7 A resolution, space group of P43212, one physiological homodimer per asymmetric unit. Structure displays distinct binding sites for thioredoxin and the glutaredoxin domain, a single glutathione disulfide reduction site in the Grx domain, and rotation of the glutaredoxin domain toward the Sec-containing redox active site
-
modeled structure is a functional dimer, and contains a Grx domain (residues 21–83), a FAD/NADPH-binding domain or TrxR domain (residues 109–450) and a dimerization domain (residues 470–598)
-
in complex with FAD, orthorhombic space group P212121, with unit-cell parameters a 84.185, b 86.47, c 183.164 A
molecular docking of inhibitory compounds into the NADPH binding site, the active site of the thioredoxin reductase domain and the glutaredoxin active site. The most favoured binding site for all compounds is the oxidized glutathione-binding pocket of the thioredoxin reductase domain
crystal structure at 2.2 A resolution of TGR, deleted in the last two residues
-
crystallization of the enzyme in complex with 1,8-naphthyridine-2 carboxylate and with the 1-(2-hydroxyethyl)piperazine derivatives, sitting drop vapor diffusion method
molecular docking of inhibitory compounds into the NADPH binding site, the active site of the thioredoxin reductase domain and the glutaredoxin active site. The most favoured binding site for all compounds is the oxidized glutathione-binding pocket of the thioredoxin reductase domain. Peptide fragments Phe505'-Leu508' and Pro572'-Thr577' play a critical role in the interactions with the inhibitors
sitting drop method