PUBLICATION
Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish
- Authors
- Blaise, M., Alsarraf, H.M., Wong, J.E., Midtgaard, S.R., Laroche, F., Schack, L., Spaink, H., Stougaard, J., Thirup, S.
- ID
- ZDB-PUB-120326-28
- Date
- 2012
- Source
- Proteins 80(6): 1694-1698 (Journal)
- Registered Authors
- Spaink, Herman P.
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Crystallography, X-Ray
- Cysteine/chemistry
- Cysteine/metabolism
- Humans
- Mice
- Models, Molecular
- Molecular Sequence Data
- Nuclear Receptor Coactivators/chemistry
- Oxidation-Reduction
- Protein Structure, Tertiary
- Proteins/chemistry
- Sequence Alignment
- Sequence Homology, Amino Acid
- Zebrafish/metabolism*
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/metabolism
- PubMed
- 22434723 Full text @ Proteins
Citation
Blaise, M., Alsarraf, H.M., Wong, J.E., Midtgaard, S.R., Laroche, F., Schack, L., Spaink, H., Stougaard, J., Thirup, S. (2012) Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish. Proteins. 80(6):1694-1698.
Abstract
Reactive oxygen species (ROS) are highly reactive byproducts of oxygen produced during normal cellular metabolism, such as respiration. Due to their high reactivity, ROS can react with lipids, proteins or nucleic acids and trigger damage to the cells.1 ROS can, for example, modify DNA and initiate tumerogenesis. Cells have developed numerous strategies to detoxify ROS and to keep ROS concentration at low level. Numerous enzymes are indeed involved in ROS processing; among them are catalase, superoxide dismutase, and peroxidase. Small compounds such as vitamin C or glutathione also play important roles in ROS protection.2
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping