|
|
| Line 3: |
Line 3: |
| | <SX load='5hi9' size='340' side='right' viewer='molstar' caption='[[5hi9]], [[Resolution|resolution]] 4.40Å' scene=''> | | <SX load='5hi9' size='340' side='right' viewer='molstar' caption='[[5hi9]], [[Resolution|resolution]] 4.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hi9]] 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=5HI9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HI9 FirstGlance]. <br> | + | <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> |
| - | </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=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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hi9 ProSAT]</span></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]] 4.4Å</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=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 == |
| - | [[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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 17: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5hi9" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5hi9" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cohen, M R]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Huynh, K W]] | + | [[Category: Cohen MR]] |
| - | [[Category: Jiansen, J]] | + | [[Category: Huynh KW]] |
| - | [[Category: Lodowski, D T]] | + | [[Category: Jiansen J]] |
| - | [[Category: Moiseenkova-Bell, V Y]] | + | [[Category: Lodowski DT]] |
| - | [[Category: Samanta, A]] | + | [[Category: Moiseenkova-Bell VY]] |
| - | [[Category: Zhou, Z H]] | + | [[Category: Samanta A]] |
| - | [[Category: Transport protein]]
| + | [[Category: Zhou ZH]] |
| - | [[Category: Trpv2 ion channel]]
| + | |
| Structural highlights
Function
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).[1] [2]
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Caterina MJ, Rosen TA, Tominaga M, Brake AJ, Julius D. A capsaicin-receptor homologue with a high threshold for noxious heat. Nature. 1999 Apr 1;398(6726):436-41. PMID:10201375 doi:http://dx.doi.org/10.1038/18906
- ↑ Stokes AJ, Shimoda LM, Koblan-Huberson M, Adra CN, Turner H. A TRPV2-PKA signaling module for transduction of physical stimuli in mast cells. J Exp Med. 2004 Jul 19;200(2):137-47. Epub 2004 Jul 12. PMID:15249591 doi:http://dx.doi.org/10.1084/jem.20032082
- ↑ Huynh KW, Cohen MR, Jiang J, Samanta A, Lodowski DT, Zhou ZH, Moiseenkova-Bell VY. Structure of the full-length TRPV2 channel by cryo-EM. Nat Commun. 2016 Mar 29;7:11130. doi: 10.1038/ncomms11130. PMID:27021073 doi:http://dx.doi.org/10.1038/ncomms11130
|
