6ot2: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==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]] 4.10&Aring;' scene=''>
+<SX load='6ot2' size='340' side='right' viewer='molstar' caption='[[6ot2]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ot2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
+<table><tr><td colspan='2'>[[6ot2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRPV3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6ot2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ot2 OCA], [https://pdbe.org/6ot2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ot2 RCSB], [https://www.ebi.ac.uk/pdbsum/6ot2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ot2 ProSAT]</span></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;">
+== Disease ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/TRPV3_HUMAN TRPV3_HUMAN] Mutilating palmoplantar keratoderma with periorificial keratotic plaques. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
-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.
+== Function ==
+[https://www.uniprot.org/uniprot/TRPV3_HUMAN TRPV3_HUMAN] Putative receptor-activated non-selective calcium permeant cation channel. It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius. Activation exhibits an outward rectification. May associate with TRPV1 and may modulate its activity. Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression (catagen).<ref>PMID:12077604</ref> <ref>PMID:12077606</ref> <ref>PMID:21593771</ref>
-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>
+==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 6ot2" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Borgnia, M J]]
+[[Category: Borgnia MJ]]
-[[Category: Borschel, W F]]
+[[Category: Borschel WF]]
-[[Category: Hsu, A L]]
+[[Category: Hsu AL]]
-[[Category: Lee, S Y]]
+[[Category: Lee S-Y]]
-[[Category: Zubcevic, L]]
+[[Category: Zubcevic L]]
-[[Category: Ion channel]]
-[[Category: Membrane protein]]
-[[Category: Membrane transport]]
-[[Category: Metal transport]]
-[[Category: Transport protein]]
-[[Category: Trp channel]]
-[[Category: Trpv channel]]