5hi9

From Proteopedia

(Difference between revisions)

Revision as of 20:11, 10 April 2020

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

5hi9, resolution 4.40Å

Structural highlights

5hi9 is a 4 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5hi9"

@@ Line 3: / Line 3: @@
 <SX load='5hi9' size='340' side='right' viewer='molstar' caption='[[5hi9]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
 == 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HI9 FirstGlance]. <br>
+<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>
-</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hi9 ProSAT]</span></td></tr>
+</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>
 </table>
 == Function ==

5hi9

From Proteopedia

Revision as of 20:11, 10 April 2020

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox