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Gewählte Publikation:

SHR Neuro Krebs Kardio Lipid

Janowski, R; Scanu, S; Niessing, D; Madl, T.
Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.
ACTA CRYSTALLOGR F. 2016; 72(Pt 10): 743-749. [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG


Autor/innen der Med Uni Graz:
Madl Tobias

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Number of Figures: 2
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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 Å resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented.

Find related publications in this database (Keywords)
phospholipid hydroperoxide glutathione peroxidase 4
reactive oxidative species
NMR spectroscopy
small-angle X-ray scattering
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