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Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.
Act. Cryst. F 72, 743-749 (2016)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
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
Volume: 72,
Issue: Pt 10,
Pages: 743-749
Publisher
Blackwell
Publishing Place
Oxford [u.a.]
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)