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5h3o
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==Structure of a eukaryotic cyclic nucleotide-gated channel== | ==Structure of a eukaryotic cyclic nucleotide-gated channel== | ||
| - | < | + | <SX load='5h3o' size='340' side='right' viewer='molstar' caption='[[5h3o]], [[Resolution|resolution]] 3.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5h3o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3O OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5h3o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H3O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3o OCA], [https://pdbe.org/5h3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h3o RCSB], [https://www.ebi.ac.uk/pdbsum/5h3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CNG_CAEEL CNG_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).<ref>PMID:21173231</ref> <ref>PMID:23664973</ref> <ref>PMID:25009271</ref> <ref>PMID:25303524</ref> <ref>PMID:8893027</ref> <ref>PMID:9486798</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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-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<ref>PMID:28099415</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5h3o" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| - | [[Category: Gong | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: Li | + | [[Category: Large Structures]] |
| - | [[Category: Li | + | [[Category: Gong Y]] |
| - | [[Category: Li | + | [[Category: Li H]] |
| - | [[Category: Michailidis | + | [[Category: Li M]] |
| - | [[Category: Su | + | [[Category: Li X]] |
| - | [[Category: Wang | + | [[Category: Michailidis I]] |
| - | [[Category: Yang | + | [[Category: Su D]] |
| - | [[Category: Zhou | + | [[Category: Wang S]] |
| - | + | [[Category: Yang J]] | |
| - | + | [[Category: Zhou X]] | |
| - | + | ||
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| - | + | ||
Current revision
Structure of a eukaryotic cyclic nucleotide-gated channel
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Categories: Caenorhabditis elegans | Large Structures | Gong Y | Li H | Li M | Li X | Michailidis I | Su D | Wang S | Yang J | Zhou X
