2a2p
From Proteopedia
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| - | [[Image:2a2p.gif|left|200px]] | + | [[Image:2a2p.gif|left|200px]] |
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| - | '''Solution structure of SelM from Mus musculus''' | + | {{Structure |
| + | |PDB= 2a2p |SIZE=350|CAPTION= <scene name='initialview01'>2a2p</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Sepm, Selm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of SelM from Mus musculus''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2A2P is a [ | + | 2A2P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2P OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16319061 16319061] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: selenoprotein]] | [[Category: selenoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:44:38 2008'' |
Revision as of 13:44, 20 March 2008
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| Gene: | Sepm, Selm (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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