6ot2: Difference between revisions
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==Structure of the TRPV3 K169A sensitized mutant in apo form at 4.1 A resolution== | |||
<StructureSection load='6ot2' size='340' side='right'caption='[[6ot2]], [[Resolution|resolution]] 4.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ot2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OT2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OT2 FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=6ot2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ot2 OCA], [http://pdbe.org/6ot2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ot2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ot2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ot2 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a b-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes. | |||
Regulatory switch at the cytoplasmic interface controls TRPV channel gating.,Zubcevic L, Borschel WF, Hsu AL, Borgnia MJ, Lee SY Elife. 2019 May 9;8. pii: 47746. doi: 10.7554/eLife.47746. PMID:31070581<ref>PMID:31070581</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ot2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Borgnia, M J]] | |||
[[Category: Borschel, W F]] | |||
[[Category: Hsu, A L]] | |||
[[Category: Lee, S Y]] | |||
[[Category: Zubcevic, L]] | |||
[[Category: Ion channel]] | |||
[[Category: Membrane protein]] | |||
[[Category: Membrane transport]] | |||
[[Category: Metal transport]] | |||
[[Category: Transport protein]] | |||
[[Category: Trp channel]] | |||
[[Category: Trpv channel]] | |||
Revision as of 09:56, 23 May 2019
Structure of the TRPV3 K169A sensitized mutant in apo form at 4.1 A resolutionStructure of the TRPV3 K169A sensitized mutant in apo form at 4.1 A resolution
Structural highlights
Publication Abstract from PubMedTemperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a b-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes. Regulatory switch at the cytoplasmic interface controls TRPV channel gating.,Zubcevic L, Borschel WF, Hsu AL, Borgnia MJ, Lee SY Elife. 2019 May 9;8. pii: 47746. doi: 10.7554/eLife.47746. PMID:31070581[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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