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首页> 外文期刊>Journal of Molecular Biology >Efficient folding of the Fc epsilon RI alpha-chain membrane-proximal domain D2 depends on the presence of the N-terminal domain D1
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Efficient folding of the Fc epsilon RI alpha-chain membrane-proximal domain D2 depends on the presence of the N-terminal domain D1

机译：FcεRIα-链膜近端结构域D2的有效折叠取决于N端结构域D1的存在

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摘要

Human high affinity receptor for IgE is a membrane glycoprotein multichain complex presenting two extracellular Ig modules in its alpha-chain (D1D2). The receptor IgE binding region is located within the membrane-proximal module D2, while the N-terminal module D1 appears, to promote an optimal receptor conformation for IgE binding. To understand the structural relationship between the two modules, we dissected FcepsilonRI alpha-chain into its discrete Ig units and expressed them in mammalian cells. Unexpectedly, D2 was secreted as a disulphide-linked dimer, while D1 was monomeric. Active secretion and full glycosylation of dimeric D2 suggest a native-like conformation of the protein, justifying the escape from the endoplasmic reticulum/Golgi quality control systems. We then propose a domain-swapping model for D2, in which two interdigitated polypeptide chains assume the overall conformation of two Ig modules, as observed for rat CD2 N-terminal domain. Fusion of an unrelated Ig fold moiety at the N terminus of D2 did not interfere with its dimerisation. While D1D2 assumes a correct fold, co-expression of both isolated domains in the same cell did not restore monomeric folding of D2. Thus, D1 appears to assist the appropriate folding of FcepsilonRI alpha-chain, acting as an uncleavable intramolecular chaperone-like block towards D2. (C) 2002 Elsevier Science Ltd. All rights reserved. [References: 43]
机译：人类对IgE的高亲和力受体是一种膜糖蛋白多链复合物，在其α链（D1D2）中具有两个细胞外Ig模块。受体IgE结合区位于膜近端模块D2内，而N端模块D1出现，以促进IgE结合的最佳受体构象。为了了解这两个模块之间的结构关系，我们将FcepsilonRIα链分解为离散的Ig单元，并在哺乳动物细胞中表达它们。出乎意料的是，D2是作为二硫键连接的二聚体而分泌的，而D1是单体的。二聚体D2的主动分泌和完全糖基化表明该蛋白具有天然的构象，证明从内质网/高尔基体质控制系统中逃逸是正确的。然后，我们提出了一个D2的域交换模型，其中两个相互交叉的多肽链假定了两个Ig模块的整体构象，如对大鼠CD2 N端域观察到的那样。不相关的Ig折叠部分在D2的N末端融合不会干扰其二聚化。虽然D1D2假定正确折叠，但同一细胞中两个分离域的共表达不能恢复D2的单体折叠。因此，D1似乎有助于FcepsilonRIα链的适当折叠，充当朝向D2的不可裂解的分子内分子伴侣状阻滞。 （C）2002 Elsevier ScienceLtd。保留所有权利。 [参考：43]

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