2a2p
From Proteopedia
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(New page: 200px<br /><applet load="2a2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a2p" /> '''Solution structure of SelM from Mus musculus...)
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Revision as of 05:45, 21 November 2007
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Solution structure of SelM from Mus musculus
Overview
Selenium has significant health benefits, including potent cancer, prevention activity and roles in immune function and the male reproductive, system. Selenium-containing proteins, which incorporate this essential, micronutrient as selenocysteine, are proposed to mediate the positive, effects of dietary selenium. Presented here are the solution NMR, structures of the selenoprotein SelM and an ortholog of the selenoprotein, Sep15. These data reveal that Sep15 and SelM are structural homologs that, establish a new thioredoxin-like protein family. The location of the, active-site redox motifs within the fold together with the observed, localized conformational changes after thiol-disulfide exchange and, measured redox potential indicate that they have redox activity. In, mammals, Sep15 expression is regulated by dietary selenium, and either, decreased or increased expression of this selenoprotein alters redox, homeostasis. A physiological role for Sep15 and SelM as thiol-disulfide, oxidoreductases and their contribution to the quality control pathways of, the endoplasmic reticulum are discussed.
About this Structure
2A2P is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family., Ferguson AD, Labunskyy VM, Fomenko DE, Arac D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J, J Biol Chem. 2006 Feb 10;281(6):3536-43. Epub 2005 Nov 30. PMID:16319061
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