1a68

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Current revision (06:27, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1a68' size='340' side='right'caption='[[1a68]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1a68' size='340' side='right'caption='[[1a68]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1a68]] 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=1A68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A68 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1a68]] 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=1A68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A68 FirstGlance]. <br>
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</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=1a68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a68 OCA], [https://pdbe.org/1a68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a68 RCSB], [https://www.ebi.ac.uk/pdbsum/1a68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a68 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a68 OCA], [https://pdbe.org/1a68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a68 RCSB], [https://www.ebi.ac.uk/pdbsum/1a68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a68 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[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=1a68 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=1a68 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Voltage-dependent, ion-selective channels such as Na+, Ca2+ and K+ channel proteins function as tetrameric assemblies of identical or similar subunits. The clustering of four subunits is thought to create an aqueous pore centred at the four-fold symmetry axis. The highly conserved, amino-terminal cytoplasmic domain (approximately 130 amino acids) immediately preceding the first putative transmembrane helix S1 is designated T1. It is known to confer specificity for tetramer formation, so the heteromeric assembly of K+-channel subunits is an important mechanism for the observed channel diversity. We have determined the crystal structure of the T1 domain of a Shaker potassium channel at 1.55 A resolution. The structure reveals that four identical subunits are arranged in a four-fold symmetry surrounding a centrally located pore about 20 A in length. Subfamily-specific assembly is provided primarily by polar interactions encoded in a conserved set of amino acids at its tetramerization interface. Most highly conserved amino acids in the T1 domain of all known potassium channels are found in the core of the protein, indicating a common structural framework for the tetramer assembly.
 
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Crystal structure of the tetramerization domain of the Shaker potassium channel.,Kreusch A, Pfaffinger PJ, Stevens CF, Choe S Nature. 1998 Apr 30;392(6679):945-8. PMID:9582078<ref>PMID:9582078</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1a68" 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]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aplca]]
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[[Category: Aplysia californica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Choe, S]]
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[[Category: Choe S]]
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[[Category: Kreusch, A]]
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[[Category: Kreusch A]]
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[[Category: Pfaffinger, P J]]
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[[Category: Pfaffinger PJ]]
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[[Category: Stevens, C F]]
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[[Category: Stevens CF]]
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[[Category: Aplysia kv1 1]]
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[[Category: Potassium channel]]
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[[Category: Tetramerization domain]]
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Current revision

CRYSTAL STRUCTURE OF THE TETRAMERIZATION DOMAIN OF THE SHAKER POTASSIUM CHANNEL

PDB ID 1a68

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