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1xsw
From Proteopedia
(Difference between revisions)
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<StructureSection load='1xsw' size='340' side='right'caption='[[1xsw]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='1xsw' size='340' side='right'caption='[[1xsw]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1xsw]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1xsw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Andma Andma]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XSW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ktx|2ktx]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ktx|2ktx]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsw OCA], [https://pdbe.org/1xsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xsw RCSB], [https://www.ebi.ac.uk/pdbsum/1xsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xsw ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:18, 3 November 2021
The solid-state NMR structure of Kaliotoxin
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Categories: Andma | Large Structures | Baldus, M | Becker, S | Giller, K | Lange, A | Pongs, O | Seidel, K | Toxin
