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==Cryo-EM structure of minimal TRPV1 with RTX bound in C1 state==
<StructureSection load='7mzc' size='340' side='right'caption='[[7mzc]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MZC 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]] 3.03&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6EU:RESINIFERATOXIN'>6EU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7mzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mzc OCA], [https://pdbe.org/7mzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mzc RCSB], [https://www.ebi.ac.uk/pdbsum/7mzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mzc ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Many transient receptor potential (TRP) channels respond to diverse stimuli and conditionally conduct small and large cations. Such functional plasticity is presumably enabled by a uniquely dynamic ion selectivity filter that is regulated by physiological agents. What is currently missing is a "photo series" of intermediate structural states that directly address this hypothesis and reveal specific mechanisms behind such dynamic channel regulation. Here, we exploit cryoelectron microscopy (cryo-EM) to visualize conformational transitions of the capsaicin receptor, TRPV1, as a model to understand how dynamic transitions of the selectivity filter in response to algogenic agents, including protons, vanilloid agonists, and peptide toxins, permit permeation by small and large organic cations. These structures also reveal mechanisms governing ligand binding substates, as well as allosteric coupling between key sites that are proximal to the selectivity filter and cytoplasmic gate. These insights suggest a general framework for understanding how TRP channels function as polymodal signal integrators.

Structural snapshots of TRPV1 reveal mechanism of polymodal functionality.,Zhang K, Julius D, Cheng Y Cell. 2021 Aug 31. pii: S0092-8674(21)00982-X. doi: 10.1016/j.cell.2021.08.012. PMID:34496225<ref>PMID:34496225</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7mzc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ion channels 3D structures|Ion channels 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Cheng Y]]
[[Category: Julius D]]
[[Category: Zhang K]]