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首页> 外文期刊>IUCrJ >Structures of three ependymin-related proteins suggest their function as a hydrophobic molecule binder
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Structures of three ependymin-related proteins suggest their function as a hydrophobic molecule binder

机译：三种与鸡薄荷素相关的蛋白质的结构表明它们具有疏水分子结合剂的功能

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Ependymin was first discovered as a predominant protein in brain extracellular fluid in fish and was suggested to be involved in functions mostly related to learning and memory. Orthologous proteins to ependymin called ependymin-related proteins (EPDRs) have been found to exist in various tissues from sea urchins to humans, yet their functional role remains to be revealed. In this study, the structures of EPDR1 from frog, mouse and human were determined and analyzed. All of the EPDR1s fold into a dimer using a monomeric subunit that is mostly made up of two stacking antiparallel β-sheets with a curvature on one side, resulting in the formation of a deep hydrophobic pocket. All six of the cysteine residues in the monomeric subunit participate in the formation of three intramolecular disulfide bonds. Other interesting features of EPDR1 include two asparagine residues with glycosylation and a Ca2+-binding site. The EPDR1 fold is very similar to the folds of bacterial VioE and LolA/LolB, which also use a similar hydrophobic pocket for their respective functions as a hydrophobic substrate-binding enzyme and a lipoprotein carrier, respectively. A further fatty-acid binding assay using EPDR1 suggests that it indeed binds to fatty acids, presumably via this pocket. Additional interactome analysis of EPDR1 showed that EPDR1 interacts with insulin-like growth factor 2 receptor and flotillin proteins, which are known to be involved in protein and vesicle translocation.
机译：Ependymin最初被发现是鱼类脑细胞外液中的主要蛋白质，并被建议参与与学习和记忆有关的功能。已经发现从海胆到人的各种组织中都存在着与依泊敏的直系同源蛋白，称为依泊敏相关蛋白（EPDRs），但其功能作用尚待揭示。在这项研究中，确定并分析了来自青蛙，小鼠和人的EPDR1的结构。所有的EPDR1s都使用一个单体亚基折叠成二聚体，该单体亚基主要由两个堆叠的反平行β-折叠片构成，在一侧弯曲，从而形成一个深的疏水袋。单体亚基中的所有六个半胱氨酸残基都参与三个分子内二硫键的形成。 EPDR1的其他有趣特征包括两个具有糖基化作用的天冬酰胺残基和一个Ca2 +结合位点。 EPDR1的折叠与细菌VioE和LolA / LolB的折叠非常相似，后者也分别使用相似的疏水袋来分别发挥疏水底物结合酶和脂蛋白载体的功能。使用EPDR1进行的另一种脂肪酸结合测定表明，它确实可以通过该口袋与脂肪酸结合。 EPDR1的其他相互作用组分析表明，EPDR1与胰岛素样生长因子2受体和弗洛蒂林蛋白相互作用，已知它们与蛋白质和囊泡移位有关。

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