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==Cryo-EM structure of full-length TRPV1 with capsaicin at 48 degrees Celsius, in an open state, class 1== | |||
<StructureSection load='7lpe' size='340' side='right'caption='[[7lpe]], [[Resolution|resolution]] 3.72Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LPE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.72Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4DY:(6E)-N-(4-HYDROXY-3-METHOXYBENZYL)-8-METHYLNON-6-ENAMIDE'>4DY</scene>, <scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene>, <scene name='pdbligand=LBN:1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine'>LBN</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=7lpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lpe OCA], [https://pdbe.org/7lpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lpe RCSB], [https://www.ebi.ac.uk/pdbsum/7lpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lpe ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Transient receptor potential vanilloid member 1 (TRPV1) is a Ca(2+)-permeable cation channel that serves as the primary heat and capsaicin sensor in humans. Using cryo-EM, we have determined the structures of apo and capsaicin-bound full-length rat TRPV1 reconstituted into lipid nanodiscs over a range of temperatures. This has allowed us to visualize the noxious heat-induced opening of TRPV1 in the presence of capsaicin. Notably, noxious heat-dependent TRPV1 opening comprises stepwise conformational transitions. Global conformational changes across multiple subdomains of TRPV1 are followed by the rearrangement of the outer pore, leading to gate opening. Solvent-accessible surface area analyses and functional studies suggest that a subset of residues form an interaction network that is directly involved in heat sensing. Our study provides a glimpse of the molecular principles underlying noxious physical and chemical stimuli sensing by TRPV1, which can be extended to other thermal sensing ion channels. | |||
Heat-dependent opening of TRPV1 in the presence of capsaicin.,Kwon DH, Zhang F, Suo Y, Bouvette J, Borgnia MJ, Lee SY Nat Struct Mol Biol. 2021 Jul;28(7):554-563. doi: 10.1038/s41594-021-00616-3., Epub 2021 Jul 8. PMID:34239123<ref>PMID:34239123</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7lpe" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Kwon DH]] | |||
[[Category: Lee S-Y]] | |||
[[Category: Suo Y]] | |||
[[Category: Zhang F]] | |||
Latest revision as of 11:57, 17 October 2024
Cryo-EM structure of full-length TRPV1 with capsaicin at 48 degrees Celsius, in an open state, class 1Cryo-EM structure of full-length TRPV1 with capsaicin at 48 degrees Celsius, in an open state, class 1
Structural highlights
Publication Abstract from PubMedTransient receptor potential vanilloid member 1 (TRPV1) is a Ca(2+)-permeable cation channel that serves as the primary heat and capsaicin sensor in humans. Using cryo-EM, we have determined the structures of apo and capsaicin-bound full-length rat TRPV1 reconstituted into lipid nanodiscs over a range of temperatures. This has allowed us to visualize the noxious heat-induced opening of TRPV1 in the presence of capsaicin. Notably, noxious heat-dependent TRPV1 opening comprises stepwise conformational transitions. Global conformational changes across multiple subdomains of TRPV1 are followed by the rearrangement of the outer pore, leading to gate opening. Solvent-accessible surface area analyses and functional studies suggest that a subset of residues form an interaction network that is directly involved in heat sensing. Our study provides a glimpse of the molecular principles underlying noxious physical and chemical stimuli sensing by TRPV1, which can be extended to other thermal sensing ion channels. Heat-dependent opening of TRPV1 in the presence of capsaicin.,Kwon DH, Zhang F, Suo Y, Bouvette J, Borgnia MJ, Lee SY Nat Struct Mol Biol. 2021 Jul;28(7):554-563. doi: 10.1038/s41594-021-00616-3., Epub 2021 Jul 8. PMID:34239123[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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