5hi9
From Proteopedia
(Difference between revisions)
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| - | '''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
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