1qdv: Difference between revisions

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New page: left|200px<br /><applet load="1qdv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qdv, resolution 1.6Å" /> '''N-TERMINAL DOMAIN, VO...
 
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[[Image:1qdv.jpg|left|200px]]<br /><applet load="1qdv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qdv, resolution 1.6&Aring;" />
'''N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131'''<br />


==Overview==
==N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131==
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.
<StructureSection load='1qdv' size='340' side='right'caption='[[1qdv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qdv]] is a 4 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=1QDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QDV FirstGlance]. <br>
</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qdv OCA], [https://pdbe.org/1qdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qdv RCSB], [https://www.ebi.ac.uk/pdbsum/1qdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qdv 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/qd/1qdv_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=1qdv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1QDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QDV OCA].
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 
== References ==
==Reference==
<references/>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11007484 11007484]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Berger JM]]
[[Category: Berger, J.M.]]
[[Category: Jan LY]]
[[Category: Jan, L.Y.]]
[[Category: Jan YN]]
[[Category: Jan, Y.N.]]
[[Category: Lin Y-F]]
[[Category: Jr., D.L.Minor.]]
[[Category: Minor Jr DL]]
[[Category: Lin, Y.F.]]
[[Category: Mobley BC]]
[[Category: Mobley, B.C.]]
[[Category: Yu M]]
[[Category: Yu, M.]]
[[Category: intracellular gate]]
[[Category: tetramer]]
[[Category: tetramerization domain]]
[[Category: voltage-gated potassium channel]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:36:40 2007''

Latest revision as of 08:15, 14 February 2024

N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131

1qdv, resolution 1.60Å

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