Structural highlights
Function
SELW_MOUSE Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Selenium is a trace element with significant biomedical potential. It is essential in mammals due to its occurrence in several proteins in the form of selenocysteine (Sec). One of the most abundant mammalian Sec-containing proteins is selenoprotein W (SelW). This protein of unknown function has a broad expression pattern and contains a candidate CXXU (where U represents Sec) redox motif. Here, we report the solution structure of the Sec13-->Cys variant of mouse SelW determined through high resolution NMR spectroscopy. The protein has a thioredoxin-like fold with the CXXU motif located in an exposed loop similarly to the redox-active site in thioredoxin. Protein dynamics studies revealed the rigidity of the protein backbone and mobility of two external loops and suggested a role of these loops in interaction with SelW partners. Molecular modeling of structures of other members of the Rdx family based on the SelW structure identified new conserved features in these proteins, including an aromatic cluster and interacting loops. Our previous study suggested an interaction between SelW and 14-3-3 proteins. In the present work, with the aid of NMR spectroscopy, we demonstrated specificity of this interaction and identified mobile loops in SelW as interacting surfaces. This finding suggests that 14-3-3 are redox-regulated proteins.
Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins.,Aachmann FL, Fomenko DE, Soragni A, Gladyshev VN, Dikiy A J Biol Chem. 2007 Dec 21;282(51):37036-44. Epub 2007 Oct 10. PMID:17928294[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jeong Dw, Kim TS, Chung YW, Lee BJ, Kim IY. Selenoprotein W is a glutathione-dependent antioxidant in vivo. FEBS Lett. 2002 Apr 24;517(1-3):225-8. PMID:12062442
- ↑ Dikiy A, Novoselov SV, Fomenko DE, Sengupta A, Carlson BA, Cerny RL, Ginalski K, Grishin NV, Hatfield DL, Gladyshev VN. SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family. Biochemistry. 2007 Jun 12;46(23):6871-82. Epub 2007 May 16. PMID:17503775 doi:http://dx.doi.org/10.1021/bi602462q
- ↑ Loflin J, Lopez N, Whanger PD, Kioussi C. Selenoprotein W during development and oxidative stress. J Inorg Biochem. 2006 Oct;100(10):1679-84. Epub 2006 Jun 17. PMID:16876868 doi:http://dx.doi.org/10.1016/j.jinorgbio.2006.05.018
- ↑ Aachmann FL, Fomenko DE, Soragni A, Gladyshev VN, Dikiy A. Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins. J Biol Chem. 2007 Dec 21;282(51):37036-44. Epub 2007 Oct 10. PMID:17928294 doi:10.1074/jbc.M705410200
