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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Crystal structure of human interferon‐γ receptor 2 reveals the structural basis for receptor specificity
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Crystal structure of human interferon‐γ receptor 2 reveals the structural basis for receptor specificity

机译：人类干扰素γ受体2应承担的晶体结构揭示了受体的结构基础特异性

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摘要

Interferon‐γ receptor 2 is a cell‐surface receptor that is required for interferon‐γ signalling and therefore plays a critical immunoregulatory role in innate and adaptive immunity against viral and also bacterial and protozoal infections. A crystal structure of the extracellular part of human interferon‐γ receptor 2 (IFNγR2) was solved by molecular replacement at 1.8?? resolution. Similar to other class 2 receptors, IFNγR2 has two fibronectin type III domains. The characteristic structural features of IFNγR2 are concentrated in its N‐terminal domain: an extensive π–cation motif of stacked residues KWRWRH, a NAG–W–NAG sandwich (where NAG stands for N ‐acetyl‐ d ‐glucosamine) and finally a helix formed by residues 78–85, which is unique among class 2 receptors. Mass spectrometry and mutational analyses showed the importance of N‐linked glycosylation to the stability of the protein and confirmed the presence of two disulfide bonds. Structure‐based bioinformatic analysis revealed independent evolutionary behaviour of both receptor domains and, together with multiple sequence alignment, identified putative binding sites for interferon‐γ and receptor 1, the ligands of IFNγR2.
机译：地理干扰素γ受体2是一个细胞表面受体这是干扰素γ信号和所需因此起着至关重要的免疫调节作用在对病毒和天然免疫与适应性免疫细菌和原生动物的感染。晶体结构的细胞外的一部分人类干扰素γ受体2(干扰素γR2)应承担的解决1.8分子替换? ?类似于其他类2受体,干扰素γR2两个纤连蛋白类型III域。干扰素γR2的结构特征,特征集中在N量终端域:一个广泛的π堆积残留的阳离子的主题KWRWRH NAG-W-NAG三明治(NAG站的地方N乙酰应承担d氨基葡萄糖)和最后一个螺旋形成的残留78 - 85,这是独一无二的中二班受体。突变分析表明的重要性N糖基化的稳定性有关蛋白质和确认两个的存在二硫键。分析发现独立的进化受体域和行为,在一起多重序列比对,确定对干扰素γ和假定的结合位点的配体受体1,干扰素γR2。

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