6ot5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "6ot5" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6ot5 is ON HOLD
+
==Structure of the TRPV3 K169A sensitized mutant in the presence of 2-APB at 3.6 A resolution==
 +
<StructureSection load='6ot5' size='340' side='right'caption='[[6ot5]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[6ot5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OT5 FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FZ4:2-aminoethyl+diphenylborinate'>FZ4</scene></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=6ot5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ot5 OCA], [http://pdbe.org/6ot5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ot5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ot5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ot5 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.
-
Authors:
+
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>
-
Description:
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 6ot5" 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 06:56, 23 May 2019

Structure of the TRPV3 K169A sensitized mutant in the presence of 2-APB at 3.6 A resolution

PDB ID 6ot5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools