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5hi9

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==Structure of the full-length TRPV2 channel by cryo-electron microscopy==
==Structure of the full-length TRPV2 channel by cryo-electron microscopy==
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<StructureSection load='5hi9' size='340' side='right' caption='[[5hi9]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
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<SX load='5hi9' size='340' side='right' viewer='molstar' caption='[[5hi9]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hi9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HI9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hi9]] 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=5HI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HI9 FirstGlance]. <br>
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</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=5hi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hi9 OCA], [http://pdbe.org/5hi9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hi9 RCSB], [http://www.ebi.ac.uk/pdbsum/5hi9 PDBsum]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hi9 OCA], [https://pdbe.org/5hi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hi9 RCSB], [https://www.ebi.ac.uk/pdbsum/5hi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hi9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a 'minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2-6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel function, we determined the structure of full-length TRPV2 at approximately 5 A resolution by cryo-electron microscopy. Like TRPV1, TRPV2 contains two constrictions, one each in the pore-forming upper and lower gates. The agonist-free full-length TRPV2 has wider upper and lower gates compared with closed and agonist-activated TRPV1. We propose these newly revealed TRPV2 structural features contribute to diversity of TRPV channels.
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Structure of the full-length TRPV2 channel by cryo-EM.,Huynh KW, Cohen MR, Jiang J, Samanta A, Lodowski DT, Zhou ZH, Moiseenkova-Bell VY Nat Commun. 2016 Mar 29;7:11130. doi: 10.1038/ncomms11130. PMID:27021073<ref>PMID:27021073</ref>
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==See Also==
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5hi9" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Cohen, M R]]
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[[Category: Large Structures]]
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[[Category: Huynh, K W]]
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[[Category: Rattus norvegicus]]
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[[Category: Jiansen, J]]
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[[Category: Cohen MR]]
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[[Category: Lodowski, D T]]
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[[Category: Huynh KW]]
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[[Category: Moiseenkova-Bell, V Y]]
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[[Category: Jiansen J]]
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[[Category: Samanta, A]]
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[[Category: Lodowski DT]]
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[[Category: Zhou, Z H]]
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[[Category: Moiseenkova-Bell VY]]
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[[Category: Transport protein]]
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[[Category: Samanta A]]
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[[Category: Trpv2 ion channel]]
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[[Category: Zhou ZH]]

Current revision

Structure of the full-length TRPV2 channel by cryo-electron microscopy

5hi9, resolution 4.40Å

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