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Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.
- Source :
-
Acta Crystallographica: Section F, Structural Biology Communications . Oct2016, Vol. 72 Issue 10, p743-749. 6p. - Publication Year :
- 2016
-
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 Å resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented. [ABSTRACT FROM AUTHOR]
- Subjects :
- *GLUTATHIONE peroxidase
*HYDROPEROXY radicals
Subjects
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 72
- Issue :
- 10
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 118585835
- Full Text :
- https://doi.org/10.1107/S2053230X16013686