TY  - JOUR
AB  - 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.
AU  - Janowski, R.
AU  - Scanu, S.
AU  - Niessing, D.
AU  - Madl, T.
C1  - 49689
C2  - 40877
CY  - Chester
SP  - 743-749
TI  - Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.
JO  - Act. Cryst. F
VL  - 72
IS  - Pt 10
PB  - Int Union Crystallography
PY  - 2016
SN  - 2053-230X
ER  -