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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural characterization of a human Fc fragment engineered for lack of effector functions
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Structural characterization of a human Fc fragment engineered for lack of effector functions

机译：结构表征人类Fc片段工程由于缺乏效应的功能

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摘要

The first three-dimensional structure of a human Fc fragment genetically engineered for the elimination of its ability to mediate antibody-dependent cell-mediated cytotoxicity and complement-dependent cytotoxicity is reported. When introduced into the lower hinge and C(H)2 domain of human IgG1 molecules, the triple mutation L234F/L235E/P331S ('TM') causes a profound decrease in their binding to human CD64, CD32A, CD16 and C1q. Enzymatically produced Fc/TM fragment was crystallized and its structure was solved at a resolution of 2.3 angstrom using molecular replacement. This study revealed that the three-dimensional structure of Fc/TM is very similar to those of other human Fc fragments in the experimentally visible region spanning residues 236-445. Thus, the dramatic broad-ranging effects of TM on IgG binding to several effector molecules cannot be explained in terms of major structural rearrangements in this portion of the Fc.
机译：第一个人类的三维结构转基因的Fc片段消除其调解的能力锁定细胞介导的细胞毒性和补体依赖细胞毒性报告。当引入低铰链和C (H) 2域的人类IgG1分子,三重突变L234F / L235E P331S (TM)引起深刻的减少人类CD64的绑定,CD32A, CD16 C1q。片段是结晶及其结构解决了在2.3埃分辨率使用分子置换。Fc / TM很的三维结构类似于其他人类Fc碎片实验可见区域跨越残留236 - 445。广泛的影响对免疫球蛋白结合TM几个效应分子无法解释主要结构的重组俱乐部的一部分。

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