Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
MOA (Marasmius oreades agglutinin), a lectin isolated from fruiting bodies of the mushroom M. oreades, specifically binds nonreducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Here, we present the crystal structure of MOA in complex with the blood group B trisaccharide solved at 1.8 A resolution. To our knowledge, this is the first blood-group-B-specific structure reported in complex with a blood group B determinant. The carbohydrate ligand binds to all three binding sites of the N-terminal beta-trefoil domain. Also, in this work, Ca(2+) was included in the crystals, and binding of Ca(2+) to the MOA homodimer altered the conformation of the C-terminal domain by opening up the cleft containing a putative catalytic site.
Structural characterization of a lectin from the mushroom Marasmius oreades in complex with the blood group B trisaccharide and calcium.,Grahn EM, Winter HC, Tateno H, Goldstein IJ, Krengel U J Mol Biol. 2009 Jul 17;390(3):457-66. Epub 2009 May 6. PMID:19426740[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grahn EM, Winter HC, Tateno H, Goldstein IJ, Krengel U. Structural characterization of a lectin from the mushroom Marasmius oreades in complex with the blood group B trisaccharide and calcium. J Mol Biol. 2009 Jul 17;390(3):457-66. Epub 2009 May 6. PMID:19426740 doi:10.1016/j.jmb.2009.04.074
