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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural transitions of complement component C3 and its activation products
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Structural transitions of complement component C3 and its activation products

机译:补体成分C3及其激活产物的结构转变

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摘要

Complement sensitizes pathogens for phagocytosis and lysis. We use electron microscopy to examine the structural transitions in the activation of the pivotal protein in the complement pathway, C3. In the cleavage product C3b, the position of the thioester domain moves ≈100 A, which becomes covalently coupled to antigenic surfaces. In the iC3b fragment, cleavage in an intervening domain creates a long flexible linker between the thioester domain and the macroglobulin domain ring of C3. Studies on two products of nucleophile addition to C3 reveal a structural intermediate in activation, and a final product, in which the anaphylatoxin domain has undergone a remarkable movement through the macroglobulin ring.
机译:补体使病原体对吞噬作用和裂解敏感。我们使用电子显微镜检查补体途径C3中关键蛋白的激活中的结构转变。在裂解产物C3b中,硫酯结构域的位置移动≈100A,它与抗原表面共价偶联。在iC3b片段中,在中间结构域中的切割在C3的硫酯结构域和巨球蛋白结构域环之间产生了一个长的柔性接头。对添加到C3的亲核试剂的两种产物的研究揭示了激活的结构中间体和最终产物,其中过敏毒素域通过巨球蛋白环经历了显着运动。

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