2X50
Crystal structure of Trypanothione reductase from Leishmania infantum in complex with NADPH and silver
Summary for 2X50
| Entry DOI | 10.2210/pdb2x50/pdb |
| Related | 2JK6 2W0H |
| Descriptor | TRYPANOTHIONE REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total) |
| Functional Keywords | fad, flavoprotein, leishmaniasis, oxidative metabolism, oxidoreductase, redox-active center |
| Biological source | LEISHMANIA INFANTUM |
| Total number of polymer chains | 2 |
| Total formula weight | 113974.31 |
| Authors | Baiocco, P.,Ilari, A.,Colotti, G. (deposition date: 2010-02-03, release date: 2011-01-12, Last modification date: 2023-12-20) |
| Primary citation | Baiocco, P.,Colotti, G.,Ilari, A. Inhibitory Effect of Silver Nanoparticles on Trypanothione Reductase Activity and Leishmania Infantum Proliferation Acs Med.Chem.Lett., 2:230-, 2011 Cited by PubMed Abstract: In Leishmania the glutathione/glutathione reductase eukaryotic redox sys-tem is replaced by the unique trypanothione/trypanothione reductase (TR) system. In vitro, silver is a more effective TR inhibitor than antimony, the first line drug against leishmaniasis in most endemic countries, and its mechanism of inhibition is similar to that of Sb(III). In particular, silver binds with high affinity to the catalytic triad Cys52, Cys57, and His461', thereby inhibiting TR. Here, Ag(0) activity was tested on the promastigote and amastigote stages of Leishmania infantum using a drug-delivery system consisting in Ag(0) nanoparticles encapsulated by ferritin molecules (PfFt-AgNPs). These were able to induce an antiproliferative effect on the parasites at metal concentrations lower than those used with antimony. PubMed: 24900299DOI: 10.1021/ML1002629 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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