This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5hi9
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the full-length TRPV2 channel by cryo-electron microscopy== | |
| + | <StructureSection load='5hi9' size='340' side='right' caption='[[5hi9]], [[Resolution|resolution]] 4.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </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> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:27021073</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5hi9" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cohen, M R]] | ||
| + | [[Category: Huynh, K W]] | ||
[[Category: Jiansen, J]] | [[Category: Jiansen, J]] | ||
| - | [[Category: | + | [[Category: Lodowski, D T]] |
| - | [[Category: | + | [[Category: Moiseenkova-Bell, V Y]] |
| - | [[Category: | + | [[Category: Samanta, A]] |
| - | [[Category: | + | [[Category: Zhou, Z H]] |
| + | [[Category: Transport protein]] | ||
| + | [[Category: Trpv2 ion channel]] | ||
Revision as of 16:13, 10 May 2016
Structure of the full-length TRPV2 channel by cryo-electron microscopy
| |||||||||||
