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==Crystal structure of the TRPV2 ion channel== | ==Crystal structure of the TRPV2 ion channel== | ||
<StructureSection load='6bwm' size='340' side='right' caption='[[6bwm]], [[Resolution|resolution]] 3.90Å' scene=''> | <StructureSection load='6bwm' size='340' side='right'caption='[[6bwm]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6bwm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BWM OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6bwm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BWM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=6bwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bwm OCA], [https://pdbe.org/6bwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bwm RCSB], [https://www.ebi.ac.uk/pdbsum/6bwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bwm ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G1SNM3_RABIT G1SNM3_RABIT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Transient receptor potential vanilloid (TRPV) channels are activated by ligands and heat and are involved in various physiological processes. In contrast to the architecturally related voltage-gated cation channels, TRPV1 and TRPV2 subtypes possess another activation gate at the selectivity filter that can open widely enough to permeate large organic cations. Despite recent structural advances, the mechanism of selectivity filter gating and permeation for both metal ions and large molecules by TRPV1 or TRPV2 is not well known. Here, we determined two crystal structures of rabbit TRPV2 in its Ca(2+)-bound and resiniferatoxin (RTx)- and Ca(2+)-bound forms, to 3.9 A and 3.1 A, respectively. Notably, our structures show that RTx binding leads to two-fold symmetric opening of the selectivity filter of TRPV2 that is wide enough for large organic cation permeation. Combined with functional characterizations, our studies reveal a structural basis for permeation of Ca(2+) and large organic cations in TRPV2. | |||
Conformational plasticity in the selectivity filter of the TRPV2 ion channel.,Zubcevic L, Le S, Yang H, Lee SY Nat Struct Mol Biol. 2018 May;25(5):405-415. doi: 10.1038/s41594-018-0059-z. Epub, 2018 Apr 30. PMID:29728656<ref>PMID:29728656</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6bwm" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Oryctolagus cuniculus]] | ||
[[Category: | [[Category: Le S]] | ||
[[Category: | [[Category: Lee SY]] | ||
[[Category: | [[Category: Yang H]] | ||
[[Category: | [[Category: Zubcevic L]] | ||
Latest revision as of 17:51, 4 October 2023
Crystal structure of the TRPV2 ion channelCrystal structure of the TRPV2 ion channel
Structural highlights
FunctionPublication Abstract from PubMedTransient receptor potential vanilloid (TRPV) channels are activated by ligands and heat and are involved in various physiological processes. In contrast to the architecturally related voltage-gated cation channels, TRPV1 and TRPV2 subtypes possess another activation gate at the selectivity filter that can open widely enough to permeate large organic cations. Despite recent structural advances, the mechanism of selectivity filter gating and permeation for both metal ions and large molecules by TRPV1 or TRPV2 is not well known. Here, we determined two crystal structures of rabbit TRPV2 in its Ca(2+)-bound and resiniferatoxin (RTx)- and Ca(2+)-bound forms, to 3.9 A and 3.1 A, respectively. Notably, our structures show that RTx binding leads to two-fold symmetric opening of the selectivity filter of TRPV2 that is wide enough for large organic cation permeation. Combined with functional characterizations, our studies reveal a structural basis for permeation of Ca(2+) and large organic cations in TRPV2. Conformational plasticity in the selectivity filter of the TRPV2 ion channel.,Zubcevic L, Le S, Yang H, Lee SY Nat Struct Mol Biol. 2018 May;25(5):405-415. doi: 10.1038/s41594-018-0059-z. Epub, 2018 Apr 30. PMID:29728656[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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