5l71
From Proteopedia
Crystal structure of mouse phospholipid hydroperoxide glutathione peroxidase 4 (GPx4)
Structural highlights
Function[GPX41_MOUSE] Protects cells against membrane lipid peroxidation and cell death (PubMed:12566075). Required for normal sperm development and male fertility (PubMed:19417079). Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development (PubMed:12566075). Protects from radiation and oxidative damage (PubMed:12566075). Essential for maturation and survival of photoreceptor cells (PubMed:22207760). Plays a role in a primary T cell response to viral and parasitic infection by protecting T cells from ferroptosis, a cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species, and by supporting T cell expansion (PubMed:25824823).[1] [2] [3] [4] [5] Publication Abstract from PubMedThe 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 A resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented. Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.,Janowski R, Scanu S, Niessing D, Madl T Acta Crystallogr F Struct Biol Commun. 2016 Oct 1;72(Pt 10):743-749. Epub 2016, Sep 22. PMID:27710939[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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