7mz7: Difference between revisions
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<StructureSection load='7mz7' size='340' side='right'caption='[[7mz7]], [[Resolution|resolution]] 3.35Å' scene=''> | <StructureSection load='7mz7' size='340' side='right'caption='[[7mz7]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MZ7 FirstGlance]. <br> | ||
</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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.35Å</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=7mz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mz7 OCA], [https://pdbe.org/7mz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mz7 RCSB], [https://www.ebi.ac.uk/pdbsum/7mz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mz7 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=7mz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mz7 OCA], [https://pdbe.org/7mz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mz7 RCSB], [https://www.ebi.ac.uk/pdbsum/7mz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mz7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 7mz7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7mz7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng | [[Category: Cheng Y]] | ||
[[Category: Julius | [[Category: Julius D]] | ||
[[Category: Zhang | [[Category: Zhang K]] | ||
Latest revision as of 11:59, 17 October 2024
Cryo-EM structure of minimal TRPV1 with 4 partially bound RTXCryo-EM structure of minimal TRPV1 with 4 partially bound RTX
Structural highlights
Publication Abstract from PubMedMany 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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