X-Ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium falciparum

GSTs catalyze the conjugation of glutathione with a wide variety of hydrophobic compounds, generally resulting in nontoxic products that can be readily eliminated. In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one GST isoenzyme (PfGST). This GST is h...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2003-11, Vol.100 (24), p.13821-13826
Hauptverfasser:	Fritz-Wolf, Karin, Becker, Andreas, Rahlfs, Stefan, Harwaldt, Petra, Schirmer, R. Heiner, Kabsch, Wolfgang, Becker, Katja
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antimalarials Antimalarials - pharmacology Atoms Biochemistry Biological Sciences Catalytic Domain Crystallography, X-Ray Crystals Dimerization Drug Design Enzyme Inhibitors - pharmacology Enzymes Formates glutathione Glutathione Transferase - antagonists & inhibitors Glutathione Transferase - chemistry Glutathione Transferase - genetics Glutathione Transferase - metabolism Goods and services tax Models, Molecular Molecules Monomers Parasites Plasmodium falciparum Plasmodium falciparum - enzymology Plasmodium falciparum - genetics Protein Structure, Quaternary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sodium
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