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《中国神经科学学会第十二届全国学术会议论文集》2017年
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Structure of a eukaryotic cyclic nucleotide-gated channel

Minghui Li  Xiaoyuan Zhou  Shu Wang  Ioannis Michailidis  Ye Gong  Deyuan Su  Huan Li  Xueming Li  Jian Yang  
【摘要】:Cyclic nucleotide-gated(CNG) channels are essential for vertebrate vision and olfaction signal transduction. They belong to the superfamily of voltage-gated ion channels and possess a voltage-sensor-like domain(VSLD), but they are not gated by transmembrane voltage, a property critical for proper phototransduction and olfactory transduction. Instead, CNG channels are gated by intracellular cyclic nucleotides, which bind to a cyclic nucleotide-binding domain in the cytoplasmic C-terminus. Rich knowledge has been gained from extensive functional investigation of CNG channels, but no high-resolution structure of a full-length eukaryotic CNG channel has been reported. We determined, by using single particle electron cryo-microscopy(cryo-EM), a 3.5 ?-resolution c GMP-bound open-state structure of a full-length CNG channel from the nematode Caenorhabditis elegans. The structure reveals several unusual/interesting features, including a non-domain swapped architecture, a segmented and restrained S4(which explains the voltage insensitivity), a short S4-S5 linker, and direct interactions between a cytoplasmic gating ring and both the pore domain and VSLD. The selectivity filter is lined by the carboxylate side chains of a functionally important glutamate and three rings of backbone carbonyls. The structure is in good agreement with CNG channel properties elucidated in functional studies and provides new insights into the allosteric mechanisms of how cyclic nucleotide binding opens the channel. The structure also provides a blueprint for understanding and investigating the functional effects of hereditary disease-causing single amino acid missense mutations, many of which are distributed in regions critical for cyclic nucleotide gating.

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