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

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, regulati...

Descripción completa

Detalles Bibliográficos
Autores principales: Janowski, Robert, Scanu, Sandra, Niessing, Dierk, Madl, Tobias
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2016
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5053159/
https://www.ncbi.nlm.nih.gov/pubmed/27710939
http://dx.doi.org/10.1107/S2053230X16013686
Descripción
Sumario: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.

Ejemplares similares