Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.
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SUBMITTER: Janowski R
PROVIDER: S-EPMC5053159 | biostudies-literature | 2016 Oct
REPOSITORIES: biostudies-literature
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Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.
Janowski Robert R Scanu Sandra S Niessing Dierk D Madl Tobias T
Acta crystallographica. Section F, Structural biology communications 20160922 Pt 10
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 mu ...[more]
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