确定 BDCA-2 和 dectin-2 二聚体中糖结合位点排列的相互作用。

IF 3.4 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Glycobiology Pub Date : 2024-10-03 DOI:10.1093/glycob/cwae082
Yu Liu, Jong-Won Kim, Hadar Feinberg, Nikeel Cull, William I Weis, Maureen E Taylor, Kurt Drickamer
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引用次数: 0

摘要

糖结合受体Dectin-2和血液树突状细胞抗原2(BDCA-2)通过细胞外碳水化合物识别结构域(CRD)结合寡糖配体,并通过Fc受体γ适配体(FcRγ)启动细胞内信号传导。Dectin-2 可刺激巨噬细胞与病原体结合,而 BDCA-2 则可调节浆细胞树突状细胞中细胞因子的产生。通过分析 BDCA-2 的天然二硫键变体,以及用 N 端二聚化结构域取代跨膜结构域以创建 dectin-2 和 BDCA-2 的胞外结构域二聚体,研究了这些受体的寡聚状态及其 CRD 的取向。对这些构建物以及先前描述的这些蛋白质的 CRD 晶体结构和 dectin-2 细胞外结构域扩展版的新结构进行的分析表明,二聚体中的 CRD 只存在有限的相互作用,但颈部区域的存在可以稳定相互作用。因此,二聚体中糖结合位点的取向有利于寡糖配体交联多个二聚体,导致 FcRγ 聚集,启动信号传导。
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Interactions that define the arrangement of sugar-binding sites in BDCA-2 and dectin-2 dimers.

The sugar-binding receptors dectin-2 and blood dendritic cell antigen 2 (BDCA-2) bind oligosaccharide ligands through extracellular carbohydrate-recognition domains (CRDs) and initiate intracellular signaling through Fc receptor γ adapters (FcRγ). Dectin-2 stimulates macrophages in response to pathogen binding while BDCA-2 modulates cytokine production in plasmacytoid dendritic cells. The oligomeric states of these receptors and the orientations of their CRDs have been investigated by analysis of a naturally occurring disulfide-bonded variant of BDCA-2 and by replacement of transmembrane domains with N-terminal dimerization domains to create extracellular domain dimers of both dectin-2 and BDCA-2. Analysis of these constructs, as well as previously described crystal structures of the CRDs from these proteins and a novel structure of an extended version of the extracellular domain of dectin-2, showed that there is only limited interaction of the CRDs in the dimers, but interactions can be stabilized by the presence of the neck region. The resulting orientation of sugar-binding sites in the dimers would favor crosslinking of multiple dimers by oligosaccharide ligands, causing clustering of FcRγ to initiate signaling.

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来源期刊
Glycobiology
Glycobiology 生物-生化与分子生物学
CiteScore
7.50
自引率
4.70%
发文量
73
审稿时长
3 months
期刊介绍: Established as the leading journal in the field, Glycobiology provides a unique forum dedicated to research into the biological functions of glycans, including glycoproteins, glycolipids, proteoglycans and free oligosaccharides, and on proteins that specifically interact with glycans (including lectins, glycosyltransferases, and glycosidases). Glycobiology is essential reading for researchers in biomedicine, basic science, and the biotechnology industries. By providing a single forum, the journal aims to improve communication between glycobiologists working in different disciplines and to increase the overall visibility of the field.
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