4B1B
Crystal structure of Plasmodium falciparum oxidised Thioredoxin Reductase at 2.9 angstrom
Summary for 4B1B
| Entry DOI | 10.2210/pdb4b1b/pdb |
| Descriptor | THIOREDOXIN REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | oxidoreductase, fad, nadph, thiol-mediated redox metabolism, class-i pyridine nucleotide-disulfide oxidoreductase, malaria |
| Biological source | PLASMODIUM FALCIPARUM |
| Cellular location | Cytoplasm (By similarity): Q25861 |
| Total number of polymer chains | 2 |
| Total formula weight | 121133.42 |
| Authors | Boumis, G.,Giardina, G.,Dimastrogiovanni, D.,Angelucci, F.,Saccoccia, F.,Brunori, M.,Bellelli, A.,Miele, A.E. (deposition date: 2012-07-09, release date: 2012-08-29, Last modification date: 2024-11-13) |
| Primary citation | Boumis, G.,Giardina, G.,Angelucci, F.,Bellelli, A.,Brunori, M.,Dimastrogiovanni, D.,Saccoccia, F.,Miele, A.E. Crystal Structure of Plasmodium Falciparum Thioredoxin Reductase, a Validated Drug Target. Biochem.Biophys.Res.Commun., 425:806-, 2012 Cited by PubMed Abstract: Plasmodium falciparum is the vector of the most prevalent and deadly form of malaria, and, among the Plasmodium species, it is the one with the highest rate of drug resistance. At the basis of a rational drug design project there is the selection and characterization of suitable target(s). Thioredoxin reductase, the first protection against reactive oxygen species in the erythrocytic phase of the parasite, is essential for its survival. Hence it represents a good target for the design of new anti-malarial active compounds. In this paper we present the first crystal structure of recombinant P. falciparum thioredoxin reductase (PfTrxR) at 2.9Å and discuss its differences with respect to the human orthologue. The most important one resides in the dimer interface, which offers a good binding site for selective non competitive inhibitors. The striking conservation of this feature among the Plasmodium parasites, but not among other Apicomplexa parasites neither in mammals, boosts its exploitability. PubMed: 22889878DOI: 10.1016/J.BBRC.2012.07.156 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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