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首页> 外文期刊>Journal of Molecular Biology >The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer
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The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer

机译：DC-SIGNR的结构及其部分重复结构域为受体四聚体的建模提供了见识

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The dendritic cell-specific ICAM-3 non-integrin (DC-SIGN) and its close relative DC-SIGNR recognize various glycoproteins, both pathogenic and of cellular, through the receptor lectin domain-mediated carbohydrate recognition. While the carbohydrate-recognition domains (CRD) exist as monomers and bind individual carbohydrates with low affinity and are permissive in nature, the full-length receptors form tetramers through their repeat domain and recognize specific ligands with high affinity. To understand the tetramer-based ligand binding avidity, we determined the crystal structure of DC-SIGNR with its last repeat region. Compared to the carbohydrate-bound CRD structure, the structure revealed conformational changes in the calcium and carbohydrate coordination loops of CRD, an additional disulfide bond between the N and the C termini of the CRD, and a helical conformation for the last repeat. On the basis of the current crystal structure and other published structures with sequence homology to the repeat domain, we generated a tetramer model for DC-SlGN/R using homology modeling and propose a ligand-recognition index to identify potential receptor ligands. Published by Elsevier Ltd.
机译：树突状细胞特异性ICAM-3非整联蛋白（DC-SIGN）及其近亲DC-SIGNR通过受体凝集素结构域介导的糖类识别识别各种致病性和细胞性糖蛋白。碳水化合物识别结构域（CRD）以单体形式存在并且以低亲和力结合各个碳水化合物，并且本质上是允许的，而全长受体则通过其重复结构域形成四聚体并以高亲和力识别特定的配体。为了了解基于四聚体的配体结合亲和力，我们确定了DC-SIGNR的晶体结构及其最后一个重复区域。与碳水化合物结合的CRD结构相比，该结构揭示了CRD的钙和碳水化合物配位环中的构象变化，CRD的N和C末端之间的另一个二硫键以及最后一个重复序列的螺旋构象。基于当前的晶体结构和与重复域具有序列同源性的其他已发表结构，我们使用同源性建模生成了DC-SlGN / R的四聚体模型，并提出了配体识别指数来识别潜在的受体配体。由Elsevier Ltd.发布

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