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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Structural insights into the interaction of human IgG1 with Fc gamma RI: no direct role of glycans in binding
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Structural insights into the interaction of human IgG1 with Fc gamma RI: no direct role of glycans in binding

机译：结构洞察人类之间的相互作用与Fc伽马RI IgG1:没有直接的角色聚糖在绑定

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摘要

The three-dimensional structure of a human IgG1 Fc fragment bound to wildtype human Fc gamma RI is reported. The structure of the corresponding complex was solved at a resolution of 2.4 angstrom using molecular replacement; this is the highest resolution achieved for an unmutated Fc gamma RI molecule. This study highlights the critical structural and functional role played by the second extracellular subdomain of Fc gamma RI. It also explains the long-known major energetic contribution of the Fc 'LLGG' motif at positions 234-237, and particularly of Leu235, via a 'lock- and-key' mechanism. Finally, a previously held belief is corrected and a differing view is offered on the recently proposed direct role of Fc carbohydrates in the corresponding interaction. Structural evidence is provided that such glycan-related effects are strictly indirect.
机译：人类IgG1 Fc的三维结构人类Fc伽马RI片段与野生型报道。2.4解决了复杂的决议使用分子替代埃;最高分辨率实现不突变FcγRI分子。关键结构和功能作用第二个细胞外Fcγ的子域名RI。精力充沛的Fc“LLGG”主题的贡献Leu235职位234 - 237,特别是,通过一个锁,和关键的机制。以前认为是纠正不同的观点是在最近提出了Fc碳水化合物的直接作用相应的交互。提供这种glycan-related效应严格的间接。

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