1dsx: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT==
-<StructureSection load='1dsx' size='340' side='right' caption='[[1dsx]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='1dsx' size='340' side='right'caption='[[1dsx]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dsx]] is a 8 chain structure with 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=1DSX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DSX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dsx]] is a 8 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=1DSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DSX FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dsx RCSB], [http://www.ebi.ac.uk/pdbsum/1dsx PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsx OCA], [https://pdbe.org/1dsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dsx RCSB], [https://www.ebi.ac.uk/pdbsum/1dsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dsx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/KCNA2_RAT KCNA2_RAT] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.<ref>PMID:7544443</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/ds/1dsx_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/1dsx_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1dsx ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However, structural alterations of these mutants leave open the question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically on residues at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel. Together, these data suggest that structural changes involving the buried polar T1 surfaces play a key role in the conformational changes leading to channel opening.
-The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel.,Minor DL, Lin YF, Mobley BC, Avelar A, Jan YN, Jan LY, Berger JM Cell. 2000 Sep 1;102(5):657-70. PMID:11007484<ref>PMID:11007484</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Potassium Channel|Potassium Channel]]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Avelar, A.]]
+[[Category: Avelar A]]
-[[Category: Berger, J M.]]
+[[Category: Berger JM]]
-[[Category: Jan, L Y.]]
+[[Category: Jan LY]]
-[[Category: Jan, Y N.]]
+[[Category: Jan YN]]
-[[Category: Lin, Y F.]]
+[[Category: Lin Y-F]]
-[[Category: Minor, D L.]]
+[[Category: Minor Jr DL]]
-[[Category: Mobley, B C.]]
+[[Category: Mobley BC]]
-[[Category: Assembly domain]]
-[[Category: Signaling protein]]
-[[Category: Tetramer]]
-[[Category: Voltage-gated potassium channel]]