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Janowski, Robert; Scanu, Sandra; Niessing, Dierk and Madl, Tobias (2016): Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4. In: Acta Crystallographica Section F: Structural Biology Communications, Vol. 72: pp. 743-749

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The mammalian glutathione peroxidase (GPx) family is a key component of the cellular antioxidative defence system. Within this family, GPx4 has unique features as it accepts a large class of hydroperoxy lipid substrates and has a plethora of biological functions, including sperm maturation, regulation of apoptosis and cerebral embryogenesis. In this paper, the structure of the cytoplasmic isoform of mouse phospholipid hydroperoxide glutathione peroxidase (O70325-2 GPx4) with selenocysteine 46 mutated to cysteine is reported solved at 1.8 angstrom resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented.

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