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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Nogo Receptor crystal structures with a native disulfide pattern suggest a novel mode of self‐interaction
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Nogo Receptor crystal structures with a native disulfide pattern suggest a novel mode of self‐interaction

机译：勿动蛋白受体与原生晶体结构二硫化模式介绍一种全新的模式自我检测交互

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摘要

The Nogo Receptor (NgR) is a glycophosphatidylinositol‐anchored cell‐surface protein and is a receptor for three myelin‐associated inhibitors of regeneration: myelin‐associated glycoprotein, Nogo66 and oligodendrocyte myelin glycoprotein. In combination with different co‐receptors, NgR mediates signalling that reduces neuronal plasticity. The available structures of the NgR ligand‐binding leucine‐rich repeat (LRR) domain have an artificial disulfide pattern owing to truncated C‐terminal construct boundaries. NgR has previously been shown to self‐associate via its LRR domain, but the structural basis of this interaction remains elusive. Here, crystal structures of the NgR LRR with a longer C‐terminal segment and a native disulfide pattern are presented. An additional C‐terminal loop proximal to the C‐terminal LRR cap is stabilized by two newly formed disulfide bonds, but is otherwise mostly unstructured in the absence of any stabilizing interactions. NgR crystallized in six unique crystal forms, three of which share a crystal‐packing interface. NgR crystal‐packing interfaces from all eight unique crystal forms are compared in order to explore how NgR could self‐interact on the neuronal plasma membrane.
机译：勿动蛋白受体(是)glycophosphatidylinositol量固定细胞的表面蛋白和受体三髓鞘再生量相关的抑制剂:髓磷脂相关的糖蛋白,应承担Nogo66和髓鞘少突细胞糖蛋白。结合不同公司应承担的受体,是介导的信号,减少神经元可塑性。配体检测绑定亮氨酸量丰富的重复(远程雷达)域由于二硫化人工模式吗截断C检测终端构造边界。曾被证明自我检测副通过吗它的远程雷达领域,但是这个的结构基础互动仍然是难以捉摸的。的结构是远程雷达和更长时间C二硫化的终端市场和本地模式提出了。近端C检测终端远程雷达帽是稳定的由两个新成立的二硫键,但是否则大部分非结构化的缺乏任何稳定的相互作用。六个独特的晶体形式,三个共享水晶填料界面。接口从所有八个独特的晶体形式比较,以探讨的是如何自我检测神经元细胞膜上的互动。

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