4B1B

Crystal structure of Plasmodium falciparum oxidised Thioredoxin Reductase at 2.9 angstrom

4B1B の概要

• エントリーDOI: 10.2210/pdb4b1b/pdb
• 分子名称: THIOREDOXIN REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase, fad, nadph, thiol-mediated redox metabolism, class-i pyridine nucleotide-disulfide oxidoreductase, malaria
• 由来する生物種: PLASMODIUM FALCIPARUM
• 細胞内の位置: Cytoplasm (By similarity): Q25861
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 121133.42

構造登録者

Boumis, G.,Giardina, G.,Dimastrogiovanni, D.,Angelucci, F.,Saccoccia, F.,Brunori, M.,Bellelli, A.,Miele, A.E. (登録日: 2012-07-09, 公開日: 2012-08-29, 最終更新日: 2024-11-13)

主引用文献

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

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: 22889878
DOI: 10.1016/J.BBRC.2012.07.156

実験手法

X-RAY DIFFRACTION (2.9 Å)