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==An unusual fold for potassium channel blockers : NMR structure of three toxins from the scorpion Opisthacanthus madagascariensis==
<StructureSection load='1wqc' size='340' side='right' caption='[[1wqc]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wqc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Opisthacanthus_madagascariensis Opisthacanthus madagascariensis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WQC FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wqd|1wqd]], [[1wqe|1wqe]]</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=1wqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wqc OCA], [http://pdbe.org/1wqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wqc RCSB], [http://www.ebi.ac.uk/pdbsum/1wqc PDBsum]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The Om-toxins are short peptides (23-27 amino acids) purified from the venom of the scorpion Opisthacanthus madagascariensis. Their pharmacological targets are thought to be potassium channels. Like Csalpha/beta (cystine-stabilized alpha/beta) toxins, the Om-toxins alter the electrophysiological properties of these channels; however, they do not share any sequence similarity with other scorpion toxins. We herein demonstrate by electrophysiological experiments that Om-toxins decrease the amplitude of the K+ current of the rat channels Kv1.1 and Kv1.2, as well as human Kv1.3. We also determine the solution structure of three of the toxins by use of two-dimensional proton NMR techniques followed by distance geometry and molecular dynamics. The structures of these three peptides display an uncommon fold for ion-channel blockers, Csalpha/alpha (cystine-stabilized alpha-helix-loop-helix), i.e. two alpha-helices connected by a loop and stabilized by two disulphide bridges. We compare the structures obtained and the dipole moments resulting from the electrostatic anisotropy of these peptides with those of the only other toxin known to share the same fold, namely kappa-hefutoxin1.

An unusual fold for potassium channel blockers: NMR structure of three toxins from the scorpion Opisthacanthus madagascariensis.,Chagot B, Pimentel C, Dai L, Pil J, Tytgat J, Nakajima T, Corzo G, Darbon H, Ferrat G Biochem J. 2005 May 15;388(Pt 1):263-71. PMID:15631621<ref>PMID:15631621</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Potassium channel toxin|Potassium channel toxin]]
== References ==
<references/>
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</StructureSection>
[[Category: Opisthacanthus madagascariensis]]
[[Category: Chagot, B]]
[[Category: Corzo, G]]
[[Category: Dai, L]]
[[Category: Darbon, H]]
[[Category: Ferrat, G]]
[[Category: Nakajima, T]]
[[Category: Pil, J]]
[[Category: Pimentel, C]]
[[Category: Tytgat, J]]
[[Category: Toxin]]