2x50

Crystal structure of Trypanothione reductase from Leishmania infantum in complex with NADPH and silverCrystal structure of Trypanothione reductase from Leishmania infantum in complex with NADPH and silver

Structural highlights 2x50 is a 2 chain structure with sequence from Leishmania infantum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3Å Ligands: , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A4HSF7_LEIIN Publication Abstract from PubMed 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. Inhibitory Effect of Silver Nanoparticles on Trypanothione Reductase Activity and Leishmania infantum Proliferation.,Baiocco P, Ilari A, Ceci P, Orsini S, Gramiccia M, Di Muccio T, Colotti G ACS Med Chem Lett. 2010 Dec 29;2(3):230-3. doi: 10.1021/ml1002629. eCollection, 2011 Mar 10. PMID:24900299 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypanothione reductase

spinqualitylabelsall models 2x50, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image