Structure of the mouse TRPC4 ion channel.

Structure of the mouse TRPC4 ion channel.
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小鼠TRPC4离子通道的结构

DOI:
10.1038/s41467-018-05247-9
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发表时间:
2018-08-06
影响因子:
16.6
通讯作者:
Zhang J
Zhang J
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Duan J;Li J;Zeng B;Chen GL;Peng X;Zhang Y;Wang J;Clapham DE;Li Z;Zhang J

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瞬时受体电位(TRP)离子通道的成员将阳离子传导到细胞中。它们介导的功能范围从神经元介导的热和冷感觉到细胞内细胞器和初级纤毛信号传导。在这里,我们报告了TRPC 4在其未配体(apo)状态下的冷冻电子显微镜(cryo-EM)结构,总分辨率为3.3 μ m。该结构揭示了一种独特的结构,具有由二硫键稳定的长孔环。除了共享的四聚体六跨膜折叠,TRPC 4结构偏离其他TRP通道具有独特的胞质结构域。这种独特的胞质N末端结构域与TRP和C末端结构域形成广泛的芳香族接触。我们的结构与其他已知的TRP结构的比较提供了分子的见解TRPC 4离子选择性,并扩展了我们的知识的多样性和演变的TRP通道。
Members of the transient receptor potential (TRP) ion channels conduct cations into cells. They mediate functions ranging from neuronally mediated hot and cold sensation to intracellular organellar and primary ciliary signaling. Here we report a cryo-electron microscopy (cryo-EM) structure of TRPC4 in its unliganded (apo) state to an overall resolution of 3.3 Å. The structure reveals a unique architecture with a long pore loop stabilized by a disulfide bond. Beyond the shared tetrameric six-transmembrane fold, the TRPC4 structure deviates from other TRP channels with a unique cytosolic domain. This unique cytosolic N-terminal domain forms extensive aromatic contacts with the TRP and the C-terminal domains. The comparison of our structure with other known TRP structures provides molecular insights into TRPC4 ion selectivity and extends our knowledge of the diversity and evolution of the TRP channels.
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发表时间: 2014-01
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影响因子: 48
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