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<StructureSection load='1eof' size='340' side='right'caption='[[1eof]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
<StructureSection load='1eof' size='340' side='right'caption='[[1eof]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1eof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplca Aplca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1eof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOF FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eod|1eod]], [[1eoe|1eoe]], [[1t1d|1t1d]]</div></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]] 2.38&#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=1eof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eof OCA], [https://pdbe.org/1eof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eof RCSB], [https://www.ebi.ac.uk/pdbsum/1eof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eof ProSAT]</span></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=1eof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eof OCA], [https://pdbe.org/1eof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eof RCSB], [https://www.ebi.ac.uk/pdbsum/1eof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eof ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q16968_APLCA Q16968_APLCA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1eof 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=1eof ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The T1 domain, a highly conserved cytoplasmic portion at the N-terminus of the voltage-dependent K+ channel (Kv) alpha-subunit, is responsible for driving and regulating the tetramerization of the alpha-subunits. Here we report the identification of a set of mutations in the T1 domain that alter the gating properties of the Kv channel. Two mutants produce a leftward shift in the activation curve and slow the channel closing rate while a third mutation produces a rightward shift in the activation curve and speeds the channel closing rate. We have determined the crystal structures of T1 domains containing these mutations. Both of the leftward shifting mutants produce similar conformational changes in the putative membrane facing surface of the T1 domain. These results suggest that the structure of the T1 domain in this region is tightly coupled to the channel's gating states.
Voltage dependent activation of potassium channels is coupled to T1 domain structure.,Cushman SJ, Nanao MH, Jahng AW, DeRubeis D, Choe S, Pfaffinger PJ Nat Struct Biol. 2000 May;7(5):403-7. PMID:10802739<ref>PMID:10802739</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1eof" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aplca]]
[[Category: Aplysia californica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Choe, S]]
[[Category: Choe S]]
[[Category: Cushman, S J]]
[[Category: Cushman SJ]]
[[Category: DeRubeis, D]]
[[Category: DeRubeis D]]
[[Category: Jahng, A W]]
[[Category: Jahng AW]]
[[Category: Nanao, M H]]
[[Category: Nanao MH]]
[[Category: Pfaffinger, P J]]
[[Category: Pfaffinger PJ]]
[[Category: Aplysia kv1 1]]
[[Category: Membrane protein]]
[[Category: Potassium channel]]
[[Category: Proton transport]]

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