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Literature summary for 1.8.1.B1 extracted from

  • Silvestri, I.; Lyu, H.; Fata, F.; Boumis, G.; Miele, A.E.; Ardini, M.; Ippoliti, R.; Bellelli, A.; Jadhav, A.; Lea, W.A.; Simeonov, A.; Cheng, Q.; Arner, E.S.J.; Thatcher, G.R.J.; Petukhov, P.A.; Williams, D.L.; Angelucci, F.
    Fragment-based discovery of a regulatory site in thioredoxin glutathione reductase acting as ''Doorstop'' for NADPH Entry (2018), ACS Chem. Biol., 13, 2190-2202 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
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 Schistosoma mansoni

Inhibitors

Inhibitors Comment Organism Structure
1,8-naphthyridine-2 carboxylate mixed inhibition. 1,8-Naphthyridine-2 carboxylate prevents Tyr296 from rotating, a process necessary for NADPH binding and enzyme reduction. It inhibits by stabilizing a protein conformation whose affinity for NADPH is greatly reduced Schistosoma mansoni

Organism

Organism UniProt Comment Textmining
Schistosoma mansoni Q962Y6
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Schistosoma mansoni

Synonyms

Synonyms Comment Organism
TGR
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 Schistosoma mansoni
thioredoxin glutathione reductase
-
 Schistosoma mansoni

General Information

General Information Comment Organism
drug target promising drug target for the treatment of schistosomiasis Schistosoma mansoni