5h3o
Structure of a eukaryotic cyclic nucleotide-gated channelStructure of a eukaryotic cyclic nucleotide-gated channel
Structural highlights
FunctionCNG_CAEEL Required for normal thermosensation and chemosensation sensory behavior (PubMed:8893027). Required, downstream of receptor-type guanylate cyclase gcy-9, for CO2-mediated responses in BAG neurons (PubMed:21173231). Required, downstream of receptor-type guanylate cyclase gcy-14, for alkaline pH-mediated responses in ASE-left (ASEL) neurons (PubMed:23664973). Involved in the development of ASJ sensory neuron axon during late larval stages and in the maintenance of normal axon morphology in the adult. Regulates dauer formation (PubMed:9486798). In ASI and ASJ sensory neurons, controls behavioral response to P.aeruginosa by up-regulating the transcription of daf-7, a member of the TGF-beta family (PubMed:25303524). In AWB and AWC sensory neurons, mediates the recognition of food oders which subsequently allows for the detection of preferred food sources (PubMed:25009271).[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedCyclic-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-A-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. Structure of a eukaryotic cyclic-nucleotide-gated channel.,Li M, Zhou X, Wang S, Michailidis I, Gong Y, Su D, Li H, Li X, Yang J Nature. 2017 Feb 2;542(7639):60-65. doi: 10.1038/nature20819. Epub 2017 Jan 18. PMID:28099415[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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