Selective Recognition of Mannose by the Human Eosinophil Charcot-Leyden Crystal Protein (Galectin-10): A Crystallographic Study at 1.8 Å Resolution.
Selective Recognition of Mannose by the Human Eosinophil Charcot-Leyden Crystal Protein (Galectin-10): A Crystallographic Study at 1.8 Å Resolution.
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DOI：
10.1021/bi990756e
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发表时间：
1999-09
期刊：
影响因子：
2.9
通讯作者：
Swaminathan;Leônidas;Savage;Ackerman;Acharya
中科院分区：
文献类型：
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作者：
Swaminathan;Leônidas;Savage;Ackerman;Acharya
嗜酸性细胞Charcot-Leyden晶体（CLC）蛋白在嗜酸性细胞或嗜碱性细胞功能或相关炎症过程中的作用尚未确定。尽管CLC蛋白已被报道表现出较弱的溶血磷脂酶活性，但它与该酶家族的任何已知成员几乎没有序列同源性。CLC蛋白的x射线晶体结构与凝集素的结构非常相似，凝集素是β-半乳糖苷特异性动物凝集素家族的成员，包括部分保守的凝集素碳水化合物识别域（CRD）。由于缺乏任何已知的这种蛋白质的天然碳水化合物配体，CLC蛋白（半乳糖凝集素-10）的功能作用仍然是推测性的。在这里，我们描述了CLC蛋白的碳水化合物结合特性的结构研究，并报道了碳水化合物与蛋白质复合物的第一个结构。有趣的是，CLC蛋白对β-半乳糖苷没有亲和力，其结合甘露糖的方式与此非常不同。
The role(s) of the eosinophil Charcot-Leyden crystal (CLC) protein in eosinophil or basophil function or associated inflammatory processes is yet to be established. Although the CLC protein has been reported to exhibit weak lysophospholipase activity, it shows virtually no sequence homology to any known member of this family of enzymes. The X-ray crystal structure of the CLC protein is very similar to the structure of the galectins, members of a β-galactoside-specific animal lectin family, including a partially conserved galectin carbohydrate recognition domain (CRD). In the absence of any known natural carbohydrate ligand for this protein, the functional role of the CLC protein (galectin-10) has remained speculative. Here we describe structural studies on the carbohydrate binding properties of the CLC protein and report the first structure of a carbohydrate in complex with the protein. Interestingly, the CLC protein demonstrates no affinity for β-galactosides and binds mannose in a manner very different ...