6oo5: Difference between revisions

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<SX load='6oo5' size='340' side='right' viewer='molstar' caption='[[6oo5]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
<SX load='6oo5' size='340' side='right' viewer='molstar' caption='[[6oo5]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6oo5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OO5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OO5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6oo5]] is a 4 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=6OO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OO5 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></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]] 4.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRPV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6oo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oo5 OCA], [http://pdbe.org/6oo5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oo5 RCSB], [http://www.ebi.ac.uk/pdbsum/6oo5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oo5 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=6oo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oo5 OCA], [https://pdbe.org/6oo5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oo5 RCSB], [https://www.ebi.ac.uk/pdbsum/6oo5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oo5 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/G1SNM3_RABIT G1SNM3_RABIT]
The Transient Receptor Potential Vanilloid 2 (TRPV2) channel is a member of the temperature-sensing thermoTRPV family. Recent advances in cryo-electronmicroscopy (cryo-EM) and X-ray crystallography have provided many important insights into the gating mechanisms of thermoTRPV channels. Interestingly, crystallographic studies of ligand-dependent TRPV2 gating have shown that the TRPV2 channel adopts two-fold symmetric arrangements during the gating cycle. However, it was unclear if crystal packing forces played a role in stabilizing the two-fold symmetric arrangement of the channel. Here we employ cryo-EM to elucidate the structure of full-length rabbit TRPV2 in complex with the agonist resiniferatoxin (RTx) in nanodiscs and amphipol. We show that RTx induces two-fold symmetric conformations of TRPV2 in both environments. However, the two-fold symmetry is more pronounced in the native-like lipid environment of the nanodiscs. Our data offers insights into a gating pathway in TRPV2 involving symmetry transitions.


Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes.,Zubcevic L, Hsu AL, Borgnia MJ, Lee SY Elife. 2019 May 15;8. pii: 45779. doi: 10.7554/eLife.45779. PMID:31090543<ref>PMID:31090543</ref>
==See Also==
 
*[[Ion channels 3D structures|Ion channels 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6oo5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: European rabbit]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Borgnia, M J]]
[[Category: Oryctolagus cuniculus]]
[[Category: Hsu, A L]]
[[Category: Borgnia MJ]]
[[Category: Lee, S Y]]
[[Category: Hsu AL]]
[[Category: Zubcevic, L]]
[[Category: Lee S-Y]]
[[Category: Calcium channel]]
[[Category: Zubcevic L]]
[[Category: Ion channel]]
[[Category: Metal transport]]
[[Category: Trp channel]]

Latest revision as of 12:24, 20 March 2024

Cryo-EM structure of the C2-symmetric TRPV2/RTx complex in amphipol resolved to 4.2 ACryo-EM structure of the C2-symmetric TRPV2/RTx complex in amphipol resolved to 4.2 A

6oo5, resolution 4.20Å

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