1fh3

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(Difference between revisions)

Current revision

NMR STRUCTURES OF LQH III ALPHA-LIKE SCORPION TOXIN FROM LEIURUS QUINQUESTRIATUS CORRESPONDING TO THE MAJOR CONFORMER IN SOLUTION

Structural highlights

1fh3 is a 1 chain structure with sequence from Leiurus quinquestriatus hebraeus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCL3_LEIHE Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The dissociation is voltage-dependent. This alpha-like toxin is highly toxic to insects and competes with LqhaIT on binding to insect sodium channels. Differs from classical anti-mammalian alpha-toxins as it inhibits sodium channel inactivation in cell bodies of hippocampus brain neurons, on which the anti-mammalian Lqh2 is inactive, and is unable to affect Nav1.2 in the rat brain, on which Lqh2 is highly active. Moreover, its pharmacological properties are unique in that its binding affinity for insect channels drops >30-fold at pH 8.5 versus pH 6.5, and its rate of association with receptor site-3 on both insect and mammalian sodium channels is 4-15-fold slower compared with LqhaIT and Lqh2.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Gilles N, Blanchet C, Shichor I, Zaninetti M, Lotan I, Bertrand D, Gordon D. A scorpion alpha-like toxin that is active on insects and mammals reveals an unexpected specificity and distribution of sodium channel subtypes in rat brain neurons. J Neurosci. 1999 Oct 15;19(20):8730-9. PMID:10516292
↑ Chen H, Gordon D, Heinemann SH. Modulation of cloned skeletal muscle sodium channels by the scorpion toxins Lqh II, Lqh III, and Lqh alphaIT. Pflugers Arch. 2000 Feb;439(4):423-32. PMID:10678738
↑ Chen H, Heinemann SH. Interaction of scorpion alpha-toxins with cardiac sodium channels: binding properties and enhancement of slow inactivation. J Gen Physiol. 2001 Jun;117(6):505-18. PMID:11382802
↑ Karbat I, Kahn R, Cohen L, Ilan N, Gilles N, Corzo G, Froy O, Gur M, Albrecht G, Heinemann SH, Gordon D, Gurevitz M. The unique pharmacology of the scorpion alpha-like toxin Lqh3 is associated with its flexible C-tail. FEBS J. 2007 Apr;274(8):1918-31. Epub 2007 Mar 9. PMID:17355257 doi:http://dx.doi.org/EJB5737
↑ Sautiere P, Cestele S, Kopeyan C, Martinage A, Drobecq H, Doljansky Y, Gordon D. New toxins acting on sodium channels from the scorpion Leiurus quinquestriatus hebraeus suggest a clue to mammalian vs insect selectivity. Toxicon. 1998 Aug;36(8):1141-54. PMID:9690781

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fh3"

Categories: Large Structures | Leiurus quinquestriatus hebraeus | Krimm I | Lancelin JM | Trivelli X

@@ Line 1: / Line 1: @@
 ==NMR STRUCTURES OF LQH III ALPHA-LIKE SCORPION TOXIN FROM LEIURUS QUINQUESTRIATUS CORRESPONDING TO THE MAJOR CONFORMER IN SOLUTION==
-<StructureSection load='1fh3' size='340' side='right'caption='[[1fh3]], [[NMR_Ensembles_of_Models | 42 NMR models]]' scene=''>
+<StructureSection load='1fh3' size='340' side='right'caption='[[1fh3]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1fh3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leiurus_quinquestriatus_hebraeus Leiurus quinquestriatus hebraeus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FH3 FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bmr|1bmr]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1fh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fh3 OCA], [https://pdbe.org/1fh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fh3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fh3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SCL3_LEIQH SCL3_LEIQH]] Binds voltage-independently at site-3 of sodium channels and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. The dissociation is voltage-dependent. This alpha-like toxin is highly toxic to insects and competes with LqhaIT on binding to insect sodium channels. Differs from classical anti-mammalian alpha-toxins as it inhibits sodium channel inactivation in cell bodies of hippocampus brain neurons, on which the anti-mammalian Lqh2 is inactive, and is unable to affect Nav1.2 in the rat brain, on which Lqh2 is highly active. Moreover, its pharmacological properties are unique in that its binding affinity for insect channels drops >30-fold at pH 8.5 versus pH 6.5, and its rate of association with receptor site-3 on both insect and mammalian sodium channels is 4-15-fold slower compared with LqhaIT and Lqh2.<ref>PMID:9690781</ref> <ref>PMID:10678738</ref> <ref>PMID:10516292</ref> <ref>PMID:11382802</ref> <ref>PMID:17355257</ref>
+[https://www.uniprot.org/uniprot/SCL3_LEIHE SCL3_LEIHE] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The dissociation is voltage-dependent. This alpha-like toxin is highly toxic to insects and competes with LqhaIT on binding to insect sodium channels. Differs from classical anti-mammalian alpha-toxins as it inhibits sodium channel inactivation in cell bodies of hippocampus brain neurons, on which the anti-mammalian Lqh2 is inactive, and is unable to affect Nav1.2 in the rat brain, on which Lqh2 is highly active. Moreover, its pharmacological properties are unique in that its binding affinity for insect channels drops >30-fold at pH 8.5 versus pH 6.5, and its rate of association with receptor site-3 on both insect and mammalian sodium channels is 4-15-fold slower compared with LqhaIT and Lqh2.<ref>PMID:10516292</ref> <ref>PMID:10678738</ref> <ref>PMID:11382802</ref> <ref>PMID:17355257</ref> <ref>PMID:9690781</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 26: / Line 26: @@
 [[Category: Large Structures]]
 [[Category: Leiurus quinquestriatus hebraeus]]
-[[Category: Krimm, I]]
+[[Category: Krimm I]]
-[[Category: Lancelin, J M]]
+[[Category: Lancelin JM]]
-[[Category: Trivelli, X]]
+[[Category: Trivelli X]]
-[[Category: Alpha-like toxin]]
-[[Category: Cis-trans isomerism]]
-[[Category: Scorpion toxin]]
-[[Category: Sodium channel inhibitor non-proline cis peptide bond]]
-[[Category: Toxin]]

1fh3

From Proteopedia

Current revision

NMR STRUCTURES OF LQH III ALPHA-LIKE SCORPION TOXIN FROM LEIURUS QUINQUESTRIATUS CORRESPONDING TO THE MAJOR CONFORMER IN SOLUTION

Structural highlights

Function

Evolutionary Conservation

References

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