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• W2016129312 startingPage "704" @default.
• W2016129312 abstract "Human infection with Toxoplasma gondii is an important cause of morbidity and mortality. Protozoan parasites such as T. gondii are incapable of de novo purine biosynthesis and must acquire purines from their host, so the purine salvage pathway offers a number of potential targets for antiparasitic chemotherapy. In T. gondii tachyzoites, adenosine is the predominantly salvaged purine nucleoside, and thus adenosine kinase is a key enzyme in the purine salvage pathway of this parasite. The structure of T. gondii adenosine kinase was solved using molecular replacement and refined by simulated annealing at 1.8 A resolution to an R-factor of 0.214. The overall structure and the active site geometry are similar to human adenosine kinase, although there are significant differences. The T. gondii adenosine kinase has several unique features compared to the human sequence, including a five-residue deletion in one of the four linking segments between the two domains, which is probably responsible for a major change in the orientation of the two domains with respect to each other. These structural differences suggest the possibility of developing specific inhibitors of the parasitic enzyme." @default.
• W2016129312 created "2016-06-24" @default.
• W2016129312 creator A5044528603 @default.
• W2016129312 creator A5067498141 @default.
• W2016129312 creator A5069174677 @default.
• W2016129312 date "2008-12-31" @default.
• W2016129312 modified "2023-09-27" @default.
• W2016129312 title "Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 Å resolution" @default.
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• W2016129312 doi "https://doi.org/10.1110/ps.9.4.704" @default.
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