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2ktx
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ktx' size='340' side='right' caption='[[2ktx]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | <StructureSection load='2ktx' size='340' side='right' caption='[[2ktx]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ktx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2ktx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Andma Andma]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KTX FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ktx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ktx RCSB], [http://www.ebi.ac.uk/pdbsum/2ktx PDBsum]</span></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ktx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktx OCA], [http://pdbe.org/2ktx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ktx RCSB], [http://www.ebi.ac.uk/pdbsum/2ktx PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2ktx" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Andma]] |
[[Category: Fernandez, I]] | [[Category: Fernandez, I]] | ||
[[Category: Gairi, M]] | [[Category: Gairi, M]] | ||
Revision as of 23:30, 9 September 2015
COMPLETE KALIOTOXIN FROM ANDROCTONUS MAURETANICUS MAURETANICUS, NMR, 18 STRUCTURES
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