Crystal structure of the Nogo-receptor-2.
Crystal structure of the Nogo-receptor-2.
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Nogo-receptor-2 的晶体结构。
DOI：
10.1002/pro.597
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Nikolov,DimitarB
中科院分区：
文献类型：
--
作者：
Semavina,Mariya;Saha,Nayanendu;Kolev,MomchilV;Goldgur,Yehuda;Giger,RomanJ;Himanen,JuhaP;Nikolov,DimitarB
机械损伤时轴突再生的抑制取决于 Nogo 受体 (NgR) 与其髓磷脂衍生配体之间的相互作用。 NgR 由富含亮氨酸的重复 (LRR) 区域和不同的“茎”区域组成，该区域被认为在不同受体亚型之间结构相似。其他人已经表明，NgR1 和 NgR2 的 LRR 和茎区在赋予体内髓磷脂相关糖蛋白 (MAG) 的结合亲和力方面具有不同的作用。在这里，我们表明，与 NgR1 或 NgR2 的分离的 LRR 区域相比，纯化的重组全长 NgR1 和 NgR2 对纯化的 MAG 保持显着更高的结合亲和力。我们还展示了 LRR 的晶体结构和 NgR2 的部分茎区域，并将其与先前报道的 NgR1 结构就两种受体亚型的不同信号传导特性进行比较。
The inhibition of axon regeneration upon mechanical injury is dependent on interactions between Nogo receptors (NgRs) and their myelin‐derived ligands. NgRs are composed of a leucine‐rich repeat (LRR) region, thought to be structurally similar among the different isoforms of the receptor, and a divergent “stalk” region. It has been shown by others that the LRR and stalk regions of NgR1 and NgR2 have distinct roles in conferring binding affinity to the myelin associated glycoprotein (MAG)in vivo. Here, we show that purified recombinant full length NgR1 and NgR2 maintain significantly higher binding affinity for purified MAG as compared to the isolated LRR region of either NgR1 or NgR2. We also present the crystal structure of the LRR and part of the stalk regions of NgR2 and compare it to the previously reported NgR1 structure with respect to the distinct signaling properties of the two receptor isoforms.