2a4h: Difference between revisions
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[[Image:2a4h.gif|left|200px]] | [[Image:2a4h.gif|left|200px]] | ||
'''Solution structure of Sep15 from Drosophila melanogaster''' | {{Structure | ||
|PDB= 2a4h |SIZE=350|CAPTION= <scene name='initialview01'>2a4h</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= Sep15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | |||
}} | |||
'''Solution structure of Sep15 from Drosophila melanogaster''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2A4H is a [ | 2A4H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A4H 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: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[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 15:45:19 2008'' |
Revision as of 16:45, 20 March 2008
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Gene: | Sep15 (Drosophila melanogaster) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Solution structure of Sep15 from Drosophila melanogaster
OverviewOverview
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 StructureAbout this Structure
2A4H is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
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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