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| [[Image:2iho.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2iho| PDB=2iho | SCENE= }} | | {{STRUCTURE_2iho| PDB=2iho | SCENE= }} |
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| '''Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc'''
| | ===Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17442345}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17442345 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17442345}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[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 Sun May 4 07:31:01 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:25:09 2008'' |