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[[Image:1cmr.png|left|200px]]


{{STRUCTURE_1cmr| PDB=1cmr |  SCENE= }}
==NMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFERRING A FUNCTIONAL SNAKE BETA-HAIRPIN INTO A SCORPION ALPHA/BETA SCAFFOLD (PH 3.5, 20C), NMR, 18 STRUCTURES==
<StructureSection load='1cmr' size='340' side='right'caption='[[1cmr]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cmr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leiurus_hebraeus Leiurus hebraeus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CMR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 18 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=1cmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmr OCA], [https://pdbe.org/1cmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cmr RCSB], [https://www.ebi.ac.uk/pdbsum/1cmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cmr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KAX11_LEIHE KAX11_LEIHE] This toxin inhibits numerous potassium channels: shaker (Ki=227 nM), Kv1.2/KCNA2 (nanomolar range), Kv1.3/KCNA3 (nanomolar range), Kv1.5/KCNA5 (Kd>100 nM), Kv1.6/KCNA6 (Ki=22 nM), KCa1.1/KCNMA1 (IC(50)=5.9 nM). It blocks channel activity by a simple bimolecular inhibition process. It also shows a weak interaction with nicotinic acetylcholine receptors (nAChR), suggesting it may weakly inhibit it (PubMed:31276191). It also exhibits pH-specific antimicrobial activities against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans (PubMed:15118082).<ref>PMID:12527813</ref> <ref>PMID:15118082</ref> <ref>PMID:20007782</ref> <ref>PMID:2477548</ref> <ref>PMID:31276191</ref> <ref>PMID:7517498</ref> <ref>PMID:8204618</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The alpha/beta scorpion fold is shared by scorpion toxins, insect defensins, and plant thionins. This small and functionally versatile template contains an alpha-helix and a triple beta-sheet linked by three disulfide bridges. With the view to introduce novel functional centers within this fold, we replaced the sequence (the cysteines and glycines excepted) of the original beta-hairpin of a scorpion toxin by the sequence of a beta-hairpin that forms part of the site by which snake neurotoxins bind to nicotinic acetylcholine receptors (AcChOR). The resulting chimeric protein, synthesized by chemical means, binds to AcChOR, though with a lower affinity than the snake toxins [Drakopoulou; E., Zinn-Justin, S., Guenneugues, M., Gilquin, B., Menez, A., &amp; Vita, C. (1996) J. Biol. Chem. 271, 11979-11987]. The work described in this paper is an attempt to clarify the structural consequences associated with the transfer of the beta-hairpin. We report the determination of the three-dimensional solution structure of the chimeric protein by proton NMR spectroscopy and molecular dynamics calculations. Comparison of the structure of the chimera with those of the scorpion alpha/beta toxin and of the snake neurotoxin shows that (i) the new protein folds as an alpha/beta motif and (ii) the beta-hairpins of the chimera and of the curaremimetic toxin adopt a similar conformation. A closer inspection of the differences between the structures of the original and transferred beta-hairpins allows rationalization of the biological properties of the chimera.


===NMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFERRING A FUNCTIONAL SNAKE BETA-HAIRPIN INTO A SCORPION ALPHA/BETA SCAFFOLD (PH 3.5, 20C), NMR, 18 STRUCTURES===
Transfer of a beta-hairpin from the functional site of snake curaremimetic toxins to the alpha/beta scaffold of scorpion toxins: three-dimensional solution structure of the chimeric protein.,Zinn-Justin S, Guenneugues M, Drakopoulou E, Gilquin B, Vita C, Menez A Biochemistry. 1996 Jul 2;35(26):8535-43. PMID:8679614<ref>PMID:8679614</ref>


{{ABSTRACT_PUBMED_8679614}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1cmr" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[1cmr]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMR OCA].
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:008679614</ref><references group="xtra"/>
__TOC__
[[Category: Drakopoulou, E.]]
</StructureSection>
[[Category: Gilquin, B.]]
[[Category: Large Structures]]
[[Category: Guenneugues, M.]]
[[Category: Leiurus hebraeus]]
[[Category: Menez, A.]]
[[Category: Drakopoulou E]]
[[Category: Vita, C.]]
[[Category: Gilquin B]]
[[Category: Zinn-Justin, S.]]
[[Category: Guenneugues M]]
[[Category: Antagonist of nicotinic acetylcholine receptor]]
[[Category: Menez A]]
[[Category: Curaremimetic protein]]
[[Category: Vita C]]
[[Category: Zinn-Justin S]]
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