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首页> 外文期刊>Molecular cell >Crystal Structure of the N-Terminal Domain of Sialoadhesin in Complex with 3' Sialyllactose at 1.85 A Resolution
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Crystal Structure of the N-Terminal Domain of Sialoadhesin in Complex with 3' Sialyllactose at 1.85 A Resolution

机译:带有3'唾液乳糖的Sialoadhesin N末端结构域在1.85 A分辨率下的晶体结构

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摘要

The structure of the functional N-terminal domain from the extracellular region of the cell surface receptor sialoadhesin has been determined in complex with the oligosaccharide 3' sialyllactose. This provides structural information for the siglec family of proteins. The structure conforms to the V-set immunoglobulin-like fold but contains several distinctive features, including an intra-β sheet disulphide and a splitting of the standard β strand G into two shorter strands. These novel features appear important in adapting the V-set fold for sialic acid-mediated recognition. Analysis of the complex with 3' sialyllactose highlights three residues, conserved throughout the siglec family, as key features of the sialic acid-binding template. The complex is representative of the functional recognition interaction with carbohydrate and as such provides detailed information for a heterotypic cell adhesion interaction.
机译:已经确定了与寡糖3'唾液乳糖复合形成的来自细胞表面受体唾液酸粘附素的细胞外区域的功能性N-末端结构域的结构。这为siglec蛋白家族提供了结构信息。该结构符合V-set免疫球蛋白样折叠,但具有几个独特的特征,包括β内片状二硫化物和标准β链G分裂为两条较短的链。这些新特征在使V-set折叠适应唾液酸介导的识别中显得很重要。具有3'唾液乳糖的复合物的分析突出了三个残基,它们是整个唾液酸家族中保守的,是唾液酸结合模板的关键特征。该复合物代表与碳水化合物的功能识别相互作用,因此提供了异型细胞粘附相互作用的详细信息。

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