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3odv
From Proteopedia
(Difference between revisions)
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<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=3odv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3odv RCSB], [http://www.ebi.ac.uk/pdbsum/3odv PDBsum]</span></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=3odv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3odv RCSB], [http://www.ebi.ac.uk/pdbsum/3odv 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 08:26, 24 December 2014
X-ray structure of kaliotoxin by racemic protein crystallography
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