View source for 7l2x


==cryo-EM structure of RTX-bound minimal TRPV1 with NMDG at state c==
<StructureSection load='7l2x' size='340' side='right'caption='[[7l2x]], [[Resolution|resolution]] 3.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L2X 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]] 3.26&#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=6IY:(10R,13S)-16-amino-13-hydroxy-7,13-dioxo-8,12,14-trioxa-13lambda~5~-phosphahexadecan-10-yl+hexadecanoate'>6IY</scene>, <scene name='pdbligand=XPJ:1-deoxy-1-(methylamino)-D-allitol'>XPJ</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=7l2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l2x OCA], [https://pdbe.org/7l2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l2x RCSB], [https://www.ebi.ac.uk/pdbsum/7l2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l2x ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 7l2x" style="background-color:#fffaf0;"></div>

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