This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2iho

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2iho" size="350" color="white" frame="true" align="right" spinBox="true" caption="2iho, resolution 2.41&Aring;" /> '''Crystal structure of...)
Line 4: Line 4:
==Overview==
==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==
==About this Structure==
Line 10: Line 10:
==Reference==
==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: Marasmius oreades]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Askarieh, G.]]
[[Category: Askarieh, G.]]
-
[[Category: Goldstein, I.J.]]
+
[[Category: Goldstein, I J.]]
[[Category: Grahn, E.]]
[[Category: Grahn, E.]]
[[Category: Holmner, A.]]
[[Category: Holmner, A.]]
[[Category: Krengel, U.]]
[[Category: Krengel, U.]]
[[Category: Tateno, H.]]
[[Category: Tateno, H.]]
-
[[Category: Winter, H.C.]]
+
[[Category: Winter, H C.]]
[[Category: beta-trefoil]]
[[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''

Revision as of 15:52, 21 February 2008


2iho, resolution 2.41Å

Drag the structure with the mouse to rotate

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

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.

About this Structure

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

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:17442345

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools