View source for 7lpc


==Cryo-EM structure of full-length TRPV1 at 48 degrees Celsius==
<StructureSection load='7lpc' size='340' side='right'caption='[[7lpc]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LPC 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]] 3.06&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>, <scene name='pdbligand=T7X:PHOSPHATIDYLINOSITOL'>T7X</scene>, <scene name='pdbligand=YFP:1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol'>YFP</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=7lpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lpc OCA], [https://pdbe.org/7lpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lpc RCSB], [https://www.ebi.ac.uk/pdbsum/7lpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lpc 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lpc" 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]]