کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2186517 | 1096064 | 2009 | 10 صفحه PDF | دانلود رایگان |

SummaryMOA (Marasmius oreades agglutinin), a lectin isolated from fruiting bodies of the mushroom M. oreades, specifically binds nonreducing terminal Galα(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galα(1,3)Galβ(1,4)GlcNAc and the branched blood group B determinant Galα(1,3)[Fucα(1,2)]Gal. Here, we present the crystal structure of MOA in complex with the blood group B trisaccharide solved at 1.8 Å 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 β-trefoil domain. Also, in this work, Ca2+ was included in the crystals, and binding of Ca2+ to the MOA homodimer altered the conformation of the C-terminal domain by opening up the cleft containing a putative catalytic site.
Journal: Journal of Molecular Biology - Volume 390, Issue 3, 17 July 2009, Pages 457–466