1ktx
From Proteopedia
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| - | {{STRUCTURE_1ktx| PDB=1ktx | SCENE= }} | ||
| - | ===KALIOTOXIN (1-37) SHOWS STRUCTURAL DIFFERENCES WITH RELATED POTASSIUM CHANNEL BLOCKERS=== | ||
| - | {{ABSTRACT_PUBMED_7524673}} | ||
| - | == | + | ==KALIOTOXIN (1-37) SHOWS STRUCTURAL DIFFERENCES WITH RELATED POTASSIUM CHANNEL BLOCKERS== |
| - | [[1ktx]] is a 1 chain structure with sequence from [ | + | <StructureSection load='1ktx' size='340' side='right'caption='[[1ktx]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ktx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Androctonus_mauritanicus_mauritanicus Androctonus mauritanicus mauritanicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KTX FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1ktx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktx OCA], [https://pdbe.org/1ktx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ktx RCSB], [https://www.ebi.ac.uk/pdbsum/1ktx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ktx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KAX31_ANDMA KAX31_ANDMA] Potent inhibitor of large conductance calcium-activated potassium channels (BK-Ca). Also binds to the dendrotoxin sensitive voltage-dependent potassium channel. It appears to block channel activity by a simple bimolecular inhibition process. Induces a transient period of fast flickering in the channel openings, followed by an almost complete blockade of the channel. Its binding affinity to rat brain synaptosomes is 5-fold higher than this of KTX-3. Binding of the toxin to the channel is associated with significant structural rearrangements in both molecules. | ||
| + | == 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/kt/1ktx_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=1ktx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Potassium channel toxin|Potassium channel toxin]] | + | *[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
[[Category: Androctonus mauritanicus mauritanicus]] | [[Category: Androctonus mauritanicus mauritanicus]] | ||
| - | [[Category: Fernandez | + | [[Category: Large Structures]] |
| - | [[Category: Giralt | + | [[Category: Fernandez I]] |
| - | [[Category: Martin-Eauclaire | + | [[Category: Giralt E]] |
| - | [[Category: Pons | + | [[Category: Martin-Eauclaire M-F]] |
| - | [[Category: | + | [[Category: Pons M]] |
| - | [[Category: | + | [[Category: Rochat H]] |
| - | [[Category: | + | [[Category: Romi R]] |
| - | [[Category: | + | [[Category: Szendefi S]] |
| + | [[Category: Van Rietschtoten J]] | ||
Current revision
KALIOTOXIN (1-37) SHOWS STRUCTURAL DIFFERENCES WITH RELATED POTASSIUM CHANNEL BLOCKERS
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