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Citation
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HERO ID
1466403
Reference Type
Journal Article
Title
Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins
Author(s)
Aachmann, FL; Fomenko, DE; Soragni, A; Gladyshev, VN; Dikiy, A
Year
2007
Is Peer Reviewed?
Yes
Journal
Journal of Biological Chemistry
ISSN:
0021-9258
EISSN:
1083-351X
Volume
282
Issue
51
Page Numbers
37036-37044
Language
English
PMID
17928294
DOI
10.1074/jbc.M705410200
Abstract
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.
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IRIS
•
RDX (121-82-4)
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PubMed
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Not relevant
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