2eta

From Proteopedia

(Difference between revisions)

Revision as of 08:50, 14 June 2018

Crystal structure of the ankyrin repeat domain of the TRPV2

Structural highlights

2eta is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2et9, 2etb, 2etc
Gene:	Trpv2, Sac2b, Vrl1 (Buffalo rat)
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The TRPV ion channels mediate responses to many sensory stimuli including heat, low pH, neuropeptides, and chemical ligands. All TRPV subfamily members contain an intracellular N-terminal ankyrin repeat domain (ARD), a prevalent protein interaction motif. The 1.6-A crystal structure of the TRPV2-ARD, with six ankyrin repeats, reveals several atypical structural features. Repeats one through three display unusually long and flexible fingers with a large number of exposed aromatic residues, whereas repeats five and six have unusually long outer helices. Furthermore, a large counterclockwise twist observed in the stacking of repeats four and five breaks the regularity of the domain, altering the shape of surfaces available for interactions with proteins or other cellular ligands. Both solution studies and crystal packing interactions indicate that the TRPV2-ARD does not form homo-oligomers, suggesting that the ARD of TRPV ion channels may be used for interactions with regulatory factors rather than in promoting tetrameric assembly of the ion channels.

Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel.,Jin X, Touhey J, Gaudet R J Biol Chem. 2006 Sep 1;281(35):25006-10. Epub 2006 Jun 29. PMID:16809337^[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
↑ Jin X, Touhey J, Gaudet R. Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J Biol Chem. 2006 Sep 1;281(35):25006-10. Epub 2006 Jun 29. PMID:16809337 doi:10.1074/jbc.C600153200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2eta"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the ankyrin repeat domain of the TRPV2==
 <StructureSection load='2eta' size='340' side='right' caption='[[2eta]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2et9|2et9]], [[2etb|2etb]], [[2etc|2etc]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trpv2, Sac2b, Vrl1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=2eta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eta OCA], [http://pdbe.org/2eta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eta RCSB], [http://www.ebi.ac.uk/pdbsum/2eta PDBsum]</span></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=2eta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eta OCA], [http://pdbe.org/2eta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eta RCSB], [http://www.ebi.ac.uk/pdbsum/2eta PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eta ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/et/2eta_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/et/2eta_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2eta

From Proteopedia

Revision as of 08:50, 14 June 2018

Crystal structure of the ankyrin repeat domain of the TRPV2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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