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Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.

Act. Cryst. F 72, 743-749 (2016)
Verlagsversion Forschungsdaten DOI
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 Å resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Nmr Spectroscopy ; Phospholipid Hydroperoxide Glutathione Peroxidase 4 ; Reactive Oxidative Species ; Small-angle X-ray Scattering; Cell-death; Gpx4; Protein; Mice; Crystallography; Refinement; Expression; Reduction; Catalysis; Insights
ISSN (print) / ISBN 2053-230X
e-ISSN 1744-3091
Quellenangaben Band: 72, Heft: Pt 10, Seiten: 743-749 Artikelnummer: , Supplement: ,
Verlag Blackwell
Verlagsort Oxford [u.a.]
Begutachtungsstatus Peer reviewed