Structural highlights
Function
A9JTH8_DANRE
Publication Abstract from PubMed
The oxidation resistance proteins (OXR) help to protect eukaryotes from reactive oxygen species. The sole C-terminal domain of the OXR, named TLDc is sufficient to perform this function. However, the mechanism by which oxidation resistance occurs is poorly understood. We present here the crystal structure of the TLDc domain of the oxidation resistance protein 2 from zebrafish. The structure was determined by X-ray crystallography to atomic resolution (0.97A) and adopts an overall globular shape. Two antiparallel beta-sheets form a central beta-sandwich, surrounded by two helices and two one-turn helices. The fold shares low structural similarity to known structures. Proteins 2012. (c) 2012 Wiley Periodicals, Inc.
Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish.,Blaise M, Alsarraf HM, Wong JE, Midtgaard SR, Laroche F, Schack L, Spaink H, Stougaard J, Thirup S Proteins. 2012 Jun;80(6):1694-8. doi: 10.1002/prot.24050. Epub 2012 Mar 20. PMID:22434723[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Blaise M, Alsarraf HM, Wong JE, Midtgaard SR, Laroche F, Schack L, Spaink H, Stougaard J, Thirup S. Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish. Proteins. 2012 Jun;80(6):1694-8. doi: 10.1002/prot.24050. Epub 2012 Mar 20. PMID:22434723 doi:10.1002/prot.24050
