2eta: Difference between revisions

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-[[Image:2eta.gif|left|200px]]
-<!--
+==Crystal structure of the ankyrin repeat domain of the TRPV2==
-The line below this paragraph, containing "STRUCTURE_2eta", creates the "Structure Box" on the page.
+<StructureSection load='2eta' size='340' side='right'caption='[[2eta]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2eta]] is a 2 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=2ETA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ETA FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=2eta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eta OCA], [https://pdbe.org/2eta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eta RCSB], [https://www.ebi.ac.uk/pdbsum/2eta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eta ProSAT]</span></td></tr>
-{{STRUCTURE_2eta|  PDB=2eta  |  SCENE=  }}
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <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>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2eta ConSurf].
+<div style="clear:both"></div>
-'''Crystal structure of the ankyrin repeat domain of the TRPV2'''
+==See Also==
+*[[Ion channels 3D structures|Ion channels 3D structures]]
+== References ==
-==Overview==
+<references/>
-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.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-ETA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ETA OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/16809337 16809337]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Gaudet R]]
-[[Category: Gaudet, R.]]
+[[Category: Jin X]]
-[[Category: Jin, X.]]
-[[Category: Ankyrin repeat domain]]
-[[Category: Trpv2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:05:34 2008''