6bo4: Difference between revisions

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<SX load='6bo4' size='340' side='right' viewer='molstar' caption='[[6bo4]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<SX load='6bo4' size='340' side='right' viewer='molstar' caption='[[6bo4]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6bo4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BO4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6BO4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6bo4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BO4 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6bo5|6bo5]]</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&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trpv2, Sac2b, Vrl1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=6bo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bo4 OCA], [https://pdbe.org/6bo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bo4 RCSB], [https://www.ebi.ac.uk/pdbsum/6bo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bo4 ProSAT]</span></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=6bo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bo4 OCA], [http://pdbe.org/6bo4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bo4 RCSB], [http://www.ebi.ac.uk/pdbsum/6bo4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bo4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TRPV2_RAT TRPV2_RAT]] Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by growth factors, like IGF1, PDGF and morphogenetic neuropeptide/head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH (By similarity).<ref>PMID:10201375</ref> <ref>PMID:15249591</ref>
[https://www.uniprot.org/uniprot/TRPV2_RAT TRPV2_RAT] Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by growth factors, like IGF1, PDGF and morphogenetic neuropeptide/head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH (By similarity).<ref>PMID:10201375</ref> <ref>PMID:15249591</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cation channels of the transient receptor potential (TRP) family serve important physiological roles by opening in response to diverse intra- and extracellular stimuli that regulate their lower or upper gates. Despite extensive studies, the mechanism coupling these gates has remained obscure. Previous structures have failed to resolve extracellular loops, known in the TRPV subfamily as 'pore turrets', which are proximal to the upper gates. We established the importance of the pore turret through activity assays and by solving structures of rat TRPV2, both with and without an intact turret at resolutions of 4.0 A and 3.6 A, respectively. These structures resolve the full-length pore turret and reveal fully open and partially open states of TRPV2, both with unoccupied vanilloid pockets. Our results suggest a mechanism by which physiological signals, such as lipid binding, can regulate the lower gate and couple to the upper gate through a pore-turret-facilitated mechanism.


Structures of TRPV2 in distinct conformations provide insight into role of the pore turret.,Dosey TL, Wang Z, Fan G, Zhang Z, Serysheva II, Chiu W, Wensel TG Nat Struct Mol Biol. 2019 Jan;26(1):40-49. doi: 10.1038/s41594-018-0168-8. Epub, 2018 Dec 31. PMID:30598551<ref>PMID:30598551</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 6bo4" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dosey, T L]]
[[Category: Rattus norvegicus]]
[[Category: Wang, Z]]
[[Category: Dosey TL]]
[[Category: Cation]]
[[Category: Wang Z]]
[[Category: Channel]]
[[Category: Membrane protein]]
[[Category: Open]]
[[Category: Trp]]

Latest revision as of 17:22, 13 March 2024

Open state structure of the full-length TRPV2 cation channel with a resolved pore turret domainOpen state structure of the full-length TRPV2 cation channel with a resolved pore turret domain

6bo4, resolution 4.00Å

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