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论文题目: |
Structure of a Eukaryotic Cyclic-nucleotide-gated Channel |
作者: |
Li M, Zhou X, Wang S, Michailidis I, Gong Y, Su D, Li H, Li X, Yang J |
联系作者: |
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发表年度: |
2017 |
DOI: |
doi:10.1038/nature20819 |
摘要: |
Cyclic-nucleotide-gated channels are essential for vision and olfaction. They belong to the voltage-gated ion channel superfamily but their activities are controlled by intracellular cyclic nucleotides instead of transmembrane voltage. Here we report a 3.5-Å-resolution single-particle electron cryo-microscopy structure of a cyclic-nucleotide-gated channel from Caenorhabditis elegans in the cyclic guanosine monophosphate (cGMP)-bound open state. The channel has an unusual voltage-sensor-like domain, accounting for its deficient voltage dependence. A carboxy-terminal linker connecting S6 and the cyclic-nucleotide-binding domain interacts directly with both the voltage-sensor-like domain and the pore domain, forming a gating ring that couples conformational changes triggered by cyclic nucleotide binding to the gate. The selectivity filter is lined by the carboxylate side chains of a functionally important glutamate and three rings of backbone carbonyls. This structure provides a new framework for understanding mechanisms of ion permeation, gating and channelopathy of cyclic-nucleotide-gated channels and cyclic nucleotide modulation of related channels. |
刊物名称: |
Nature |
论文出处: |
http://www.nature.com/nature/journal/vaop/ncurrent/pdf/nature20819.pdf |
影响因子: |
38.138(2015年) |
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