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==Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins==
<StructureSection load='1wpd' size='340' side='right'caption='[[1wpd]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wpd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Heterometrus_spinifer Heterometrus spinifer] and [https://en.wikipedia.org/wiki/Scorpio_palmatus Scorpio palmatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WPD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1wpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpd OCA], [https://pdbe.org/1wpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wpd RCSB], [https://www.ebi.ac.uk/pdbsum/1wpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wpd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KAX62_SCOPA KAX62_SCOPA] Blocks voltage-gated potassium channels Kv1.2/KCNA2 (IC(50)=0.12-0.8 nM), KCa3.1/KCNN4 (IC(50)=1-2.2 nM), Shaker B (IC(50)=2.39-80 nM), Kv1.1/KCNA1 (IC(50)=37-45 or no activity, depending on the study), Kv1.3/KCNA3 (IC(50)=150-180 or no activity, depending on the study).<ref>PMID:10888198</ref> <ref>PMID:10920011</ref> <ref>PMID:12527813</ref> <ref>PMID:15498765</ref> <ref>PMID:18042681</ref> <ref>PMID:9022673</ref> <ref>PMID:9136903</ref> 
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== Publication Abstract from PubMed ==
Maurotoxin (MTX) and HsTx1 are two scorpion toxins belonging to the alpha-KTx6 structural family. These 34-residue toxins, cross-linked by four disulfide bridges, share 59% sequence identity and fold along the classical alpha/beta scaffold. Despite these structural similarities, they fully differ in their pharmacological profiles. MTX is highly active on small (SK) and intermediate (IK) conductance Ca(2+)-activated (K(+)) channels and on voltage-gated Kv1.2 channel, whereas HsTx1 potently blocks voltage-gated Kv1.1 and Kv1.3 channels only. Here, we designed and chemically produced MTX-HsTx1, a chimera of both toxins that contains the N-terminal helical region of MTX (sequence 1-16) and the C-terminal beta-sheet region of HsTx1 (sequence 17-34). The three-dimensional structure of the peptide in solution was solved by (1)H NMR. MTX-HsTx1 displays the activity of MTX on SK channel, whereas it exhibits the pharmacological profile of HsTx1 on Kv1.1, Kv1.2, Kv1.3, and IK channels. These data demonstrate that the helical region of MTX exerts a key role in SK channel recognition, whereas the beta-sheet region of HsTx1 is crucial for activity on all other channel types tested.

Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins.,Regaya I, Beeton C, Ferrat G, Andreotti N, Darbon H, De Waard M, Sabatier JM J Biol Chem. 2004 Dec 31;279(53):55690-6. Epub 2004 Oct 21. PMID:15498765<ref>PMID:15498765</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1wpd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Heterometrus spinifer]]
[[Category: Large Structures]]
[[Category: Scorpio palmatus]]
[[Category: Andreotti N]]
[[Category: Beeton C]]
[[Category: Chandy GK]]
[[Category: Darbon H]]
[[Category: De Waard M]]
[[Category: Ferrat G]]
[[Category: Regaya I]]
[[Category: Sabatier JM]]