8on9

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Current revision (14:45, 6 November 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8on9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8on9 OCA], [https://pdbe.org/8on9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8on9 RCSB], [https://www.ebi.ac.uk/pdbsum/8on9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8on9 ProSAT]</span></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=8on9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8on9 OCA], [https://pdbe.org/8on9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8on9 RCSB], [https://www.ebi.ac.uk/pdbsum/8on9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8on9 ProSAT]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rapid signaling between neurons is mediated by ligand-gated ion channels, cell-surface proteins with an extracellular ligand-binding domain and a membrane-spanning ion channel domain. The degenerin/epithelial sodium channel (DEG/ENaC) superfamily is diverse in terms of its gating stimuli, with some DEG/ENaCs gated by neuropeptides, and others gated by pH, mechanical force or enzymatic activity. The mechanism by which ligands bind to and activate DEG/ENaCs is poorly understood. Here we dissected the structural basis for neuropeptide-gated activity of a neuropeptide-gated DEG/ENaC, FMRFamide-gated sodium channel 1 (FaNaC1) from the annelid worm Malacoceros fuliginosus, using cryo-electron microscopy. Structures of FaNaC1 in the ligand-free resting state and in several ligand-bound states reveal the ligand-binding site and capture the ligand-induced conformational changes of channel gating, which we verified with complementary mutagenesis experiments. Our results illuminate channel gating in DEG/ENaCs and offer a structural template for experimental dissection of channel pharmacology and ion conduction.
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Structural basis for excitatory neuropeptide signaling.,Kalienkova V, Dandamudi M, Paulino C, Lynagh T Nat Struct Mol Biol. 2024 Apr;31(4):717-726. doi: 10.1038/s41594-023-01198-y. , Epub 2024 Feb 9. PMID:38337033<ref>PMID:38337033</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8on9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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Current revision

ASSFVRIa-bound Malacoceros FaNaC1 in lipid nanodiscs

PDB ID 8on9

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