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

Janowski, Robert; Scanu, Sandra; Niessing, Dierk und Madl, Tobias (2016): Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4. In: Acta Crystallographica Section F: Structural Biology Communications, Bd. 72: S. 743-749

Abstract

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 angstrom resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented.

• Dokumententyp: Zeitschriftenartikel
• Fakultät: Medizin
• Themengebiete: 600 Technik, Medizin, angewandte Wissenschaften > 610 Medizin und Gesundheit
• ISSN: 2053-230X
• Sprache: Englisch