Crystal structure of the Marasmius oreades mushroom lectin in complex with a Xenotransplantation epitope
Crystal structure of the Marasmius oreades mushroom lectin in complex with a Xenotransplantation epitope
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DOI：
10.1016/j.jmb.2007.03.016
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发表时间：
2007-06-08
影响因子：
5.6
通讯作者：
Krengel, Ute
中科院分区：
文献类型：
--
作者：
Grahn, Elin;Askarieh, Glareh;Krengel, Ute
MOA是一种来自蘑菇Marasmius oreades的凝集素，是少数几种特异性凝集血型B红细胞的试剂之一。此外，它是唯一已知对含Gal α（1，3）Gal的糖表位具有排他性特异性的凝集素，所述糖表位是对动物至人器官移植构成严重障碍的抗原。我们在这里描述的结构MOA在2.4埃分辨率，在复杂的线性三糖半乳糖α-（1，3）半乳糖β（1，4）GlcNAc。该结构是二聚体，每个原聚体具有两个不同的结构域：N-末端凝集素模块采用蓖麻毒素B/β-三叶折叠，并含有三个推定的碳水化合物结合位点，而C-末端结构域作为二聚化界面。后者的结构域，它有一个未知的功能，揭示了一个新的折叠与有趣的保护活性位点裂缝。许多迹象表明，MOA可能具有酶的功能，除了糖结合的性质。(c)2007爱思唯尔有限公司保留所有权利。
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 Gal alpha(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 angstrom resolution, in complex with the linear trisaccharide Gal alpha-(1,3) Gal beta(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. (c) 2007 Elsevier Ltd. All rights reserved.