Selected Publication:
SHR
Neuro
Cancer
Cardio
Lipid
Metab
Microb
Janowski, R; Scanu, S; Niessing, D; Madl, T.
Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.
Acta Crystallogr F Struct Biol Commun. 2016; 72(Pt 10):743-749
Doi: 10.1107/S2053230X16013686
[OPEN ACCESS]
Web of Science
PubMed
FullText
FullText_MUG
- Leading authors Med Uni Graz
-
Madl Tobias
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- 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.
- Find related publications in this database (using NLM MeSH Indexing)
-
Amino Acid Sequence -
-
Animals -
-
Cloning, Molecular -
-
Crystallography, X-Ray -
-
Cysteine - chemistry
-
Cysteine - metabolism
-
Escherichia coli - genetics
-
Escherichia coli - metabolism
-
Gene Expression -
-
Glutathione Peroxidase - chemistry
-
Glutathione Peroxidase - genetics
-
Glutathione Peroxidase - metabolism
-
Mice -
-
Models, Molecular -
-
Mutation -
-
Plasmids - chemistry
-
Plasmids - metabolism
-
Protein Conformation, alpha-Helical -
-
Protein Conformation, beta-Strand -
-
Protein Interaction Domains and Motifs -
-
Recombinant Proteins - chemistry
-
Recombinant Proteins - genetics
-
Recombinant Proteins - metabolism
-
Selenocysteine - chemistry
-
Selenocysteine - metabolism
-
Substrate Specificity -
- Find related publications in this database (Keywords)
-
phospholipid hydroperoxide glutathione peroxidase 4
-
reactive oxidative species
-
NMR spectroscopy
-
small-angle X-ray scattering