6oo7: Difference between revisions
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The | ==Cryo-EM structure of the C2-symmetric TRPV2/RTx complex in nanodiscs== | ||
<StructureSection load='6oo7' size='340' side='right'caption='[[6oo7]], [[Resolution|resolution]] 3.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6oo7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OO7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6oo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oo7 OCA], [http://pdbe.org/6oo7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oo7 RCSB], [http://www.ebi.ac.uk/pdbsum/6oo7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oo7 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6oo7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Borgnia, M J]] | |||
[[Category: Hsu, A L]] | |||
[[Category: Lee, S Y]] | |||
[[Category: Zubcevic, L]] | |||
[[Category: Calcium channel]] | |||
[[Category: Ion channel]] | |||
[[Category: Metal transport]] | |||
[[Category: Trp channel]] | |||
Revision as of 09:18, 29 May 2019
Cryo-EM structure of the C2-symmetric TRPV2/RTx complex in nanodiscsCryo-EM structure of the C2-symmetric TRPV2/RTx complex in nanodiscs
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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