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.
| Item Type: | Journal article |
|---|---|
| Faculties: | Medicine |
| Subjects: | 600 Technology > 610 Medicine and health |
| ISSN: | 2053-230X |
| Language: | English |
| Item ID: | 44875 |
| Date Deposited: | 27. Apr 2018 08:07 |
| Last Modified: | 04. Nov 2020 13:21 |
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