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J. Biol. Chem., Vol. 282, Issue 51, 37036-37044, December 21, 2007

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Solution Structure of Selenoprotein W and NMR Analysis of Its Interaction with 14-3-3 Proteins^*

Finn L. Aachmann, Dmitri E. Fomenko, Alice Soragni, Vadim N. Gladyshev, and Alexander Dikiy¹

From the Department of Biotechnology, Norwegian University of Science and Technology, N-7491 Trondheim, Norway and the Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588

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.

Received for publication, July 2, 2007 , and in revised form, September 21, 2007.

The atomic coordinates and structure factors (code 2NPB) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This research was supported by the faculty of Natural Sciences and Technology at the Norwegian University of Science and Technology and National Institutes of Health Grant GM061603. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ To whom correspondence should be addressed. Tel.: 47735-97863; Fax: 47735-91283; E-mail: alex.dikiy{at}biotech.ntnu.no.

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