2iho: Difference between revisions

Revision as of 18:52, 21 February 2008

Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc

OverviewOverview

MOA, a lectin from the mushroom Marasmius oreades, is one of the few reagents that specifically agglutinate blood group B erythrocytes. Further, it is the only lectin known to have exclusive specificity for Galalpha(1,3)Gal-containing sugar epitopes, which are antigens that pose a severe barrier to animal-to-human organ transplantation. We describe here the structure of MOA at 2.4 A resolution, in complex with the linear trisaccharide Galalpha(1,3)Galbeta(1,4)GlcNAc. The structure is dimeric, with two distinct domains per protomer: the N-terminal lectin module adopts a ricinB/beta-trefoil fold and contains three putative carbohydrate-binding sites, while the C-terminal domain serves as a dimerization interface. This latter domain, which has an unknown function, reveals a novel fold with intriguing conservation of an active site cleft. A number of indications suggest that MOA may have an enzymatic function in addition to the sugar-binding properties.

About this StructureAbout this Structure

2IHO is a Single protein structure of sequence from Marasmius oreades. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope., Grahn E, Askarieh G, Holmner A, Tateno H, Winter HC, Goldstein IJ, Krengel U, J Mol Biol. 2007 Jun 8;369(3):710-21. Epub 2007 Mar 15. PMID:17442345

Page seeded by OCA on Thu Feb 21 17:52:47 2008

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 ==Overview==
-MOA, a lectin from the mushroom Marasmius oreades, is one of the few, reagents that specifically agglutinate blood group B erythrocytes., Further, it is the only lectin known to have exclusive specificity for, Galalpha(1,3)Gal-containing sugar epitopes, which are antigens that pose a, severe barrier to animal-to-human organ transplantation. We describe here, the structure of MOA at 2.4 A resolution, in complex with the linear, trisaccharide Galalpha(1,3)Galbeta(1,4)GlcNAc. The structure is dimeric, with two distinct domains per protomer: the N-terminal lectin module, adopts a ricinB/beta-trefoil fold and contains three putative, carbohydrate-binding sites, while the C-terminal domain serves as a, dimerization interface. This latter domain, which has an unknown function, reveals a novel fold with intriguing conservation of an active site cleft., A number of indications suggest that MOA may have an enzymatic function in, addition to the sugar-binding properties.
+MOA, a lectin from the mushroom Marasmius oreades, is one of the few reagents that specifically agglutinate blood group B erythrocytes. Further, it is the only lectin known to have exclusive specificity for Galalpha(1,3)Gal-containing sugar epitopes, which are antigens that pose a severe barrier to animal-to-human organ transplantation. We describe here the structure of MOA at 2.4 A resolution, in complex with the linear trisaccharide Galalpha(1,3)Galbeta(1,4)GlcNAc. The structure is dimeric, with two distinct domains per protomer: the N-terminal lectin module adopts a ricinB/beta-trefoil fold and contains three putative carbohydrate-binding sites, while the C-terminal domain serves as a dimerization interface. This latter domain, which has an unknown function, reveals a novel fold with intriguing conservation of an active site cleft. A number of indications suggest that MOA may have an enzymatic function in addition to the sugar-binding properties.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Crystal structure of the marasmius oreades mushroom lectin in complex with a xenotransplantation epitope., Grahn E, Askarieh G, Holmner A, Tateno H, Winter HC, Goldstein IJ, Krengel U, J Mol Biol. 2007 Jun 8;369(3):710-21. Epub 2007 Mar 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17442345 17442345]
+Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope., Grahn E, Askarieh G, Holmner A, Tateno H, Winter HC, Goldstein IJ, Krengel U, J Mol Biol. 2007 Jun 8;369(3):710-21. Epub 2007 Mar 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17442345 17442345]
 [[Category: Marasmius oreades]]
 [[Category: Single protein]]
 [[Category: Askarieh, G.]]
-[[Category: Goldstein, I.J.]]
+[[Category: Goldstein, I J.]]
 [[Category: Grahn, E.]]
 [[Category: Holmner, A.]]
 [[Category: Krengel, U.]]
 [[Category: Tateno, H.]]
-[[Category: Winter, H.C.]]
+[[Category: Winter, H C.]]
 [[Category: beta-trefoil]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:03:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:47 2008''