3b29
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/LTC4S_HUMAN LTC4S_HUMAN] Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4. | [https://www.uniprot.org/uniprot/LTC4S_HUMAN LTC4S_HUMAN] Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Dodecyl-beta-D-selenomaltoside (SeDDM) is a seleno-detergent with a beta-glycosidic seleno-ether in place of the ether moiety in dodecyl-beta-D-maltoside. Seleno-detergents are candidates for heavy-atom agents in experimental phasing of membrane proteins in protein crystallography. Crystals of a nuclear membrane-embedded enzyme, leukotriene C(4) synthase (LTC(4)S), in complex with SeDDM were prepared and a multiwavelength anomalous diffraction (MAD) experiment was performed. The SeDDM in the LTC(4)S crystal exhibited sufficient anomalous diffraction for determination of the structure using MAD phasing. | ||
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| - | Seleno-detergent MAD phasing of leukotriene C4 synthase in complex with dodecyl-beta-D-selenomaltoside.,Saino H, Ago H, Ukita Y, Miyano M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1666-73., Epub 2011 Nov 29. PMID:22139193<ref>PMID:22139193</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3b29" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Leukotriene C4 synthase|Leukotriene C4 synthase]] | *[[Leukotriene C4 synthase|Leukotriene C4 synthase]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Human leukotriene C4 synthase in complex with dodecyl-beta-D-selenomaltoside
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