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- | {{Seed}} | |
- | [[Image:1txm.png|left|200px]] | |
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- | <!-- | + | ==SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAURUS, NMR, 35 STRUCTURES== |
- | The line below this paragraph, containing "STRUCTURE_1txm", creates the "Structure Box" on the page.
| + | <StructureSection load='1txm' size='340' side='right'caption='[[1txm]]' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1txm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scorpio_maurus Scorpio maurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXM FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 35 models</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> |
- | {{STRUCTURE_1txm| PDB=1txm | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1txm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txm OCA], [https://pdbe.org/1txm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1txm RCSB], [https://www.ebi.ac.uk/pdbsum/1txm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txm 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> |
| + | <div style="background-color:#fffaf0;"> |
| + | == Publication Abstract from PubMed == |
| + | Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1 (Kd = 37 nM), Kv1.2 (Kd = 0.8 nM), Kv1.3 (Kd = 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activated potassium channels. It has a unique disulfide pairing among the scorpion toxins family. The solution structure of MTX has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a bended helix from residues 6 to 16 connected by a loop to a two-stranded antiparallel beta sheet (residues 23 to 26 and 28 to 31). The interaction of MTX with the pore region of the Kv1.2 potassium channel has been modeled according to their charge anisotropy. The structure of MTX is similar to other short scorpion toxins despite its peculiar disulfide pairing. Its interaction with the Kv1.2 channel involves a dipole moment, which guides and orients the toxin onto the pore, toward the binding site, and which thus is responsible for the specificity. |
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- | ===SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAURUS, NMR, 35 STRUCTURES===
| + | Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels.,Blanc E, Sabatier JM, Kharrat R, Meunier S, el Ayeb M, Van Rietschoten J, Darbon H Proteins. 1997 Nov;29(3):321-33. PMID:9365987<ref>PMID:9365987</ref> |
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> |
| + | <div class="pdbe-citations 1txm" style="background-color:#fffaf0;"></div> |
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- | <!--
| + | ==See Also== |
- | The line below this paragraph, {{ABSTRACT_PUBMED_9365987}}, adds the Publication Abstract to the page
| + | *[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] |
- | (as it appears on PubMed at http://www.pubmed.gov), where 9365987 is the PubMed ID number.
| + | == References == |
- | -->
| + | <references/> |
- | {{ABSTRACT_PUBMED_9365987}}
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure== | + | [[Category: Large Structures]] |
- | 1TXM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Scorpio_maurus Scorpio maurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXM OCA].
| + | |
- | | + | |
- | ==Reference== | + | |
- | Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels., Blanc E, Sabatier JM, Kharrat R, Meunier S, el Ayeb M, Van Rietschoten J, Darbon H, Proteins. 1997 Nov;29(3):321-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9365987 9365987]
| + | |
| [[Category: Scorpio maurus]] | | [[Category: Scorpio maurus]] |
- | [[Category: Single protein]] | + | [[Category: Blanc E]] |
- | [[Category: Ayeb, M El.]] | + | [[Category: Darbon H]] |
- | [[Category: Blanc, E.]] | + | [[Category: El Ayeb M]] |
- | [[Category: Darbon, H.]]
| + | [[Category: Kharrat R]] |
- | [[Category: Kharrat, R.]] | + | [[Category: Meunier S]] |
- | [[Category: Meunier, S.]] | + | [[Category: Sabatier J-M]] |
- | [[Category: Rietschoten, J Van.]]
| + | [[Category: Van Rietschoten J]] |
- | [[Category: Sabatier, J M.]] | + | |
- | [[Category: Alpha beta scorpion toxin fold]] | + | |
- | [[Category: Neurotoxin]]
| + | |
- | [[Category: Potassium channel blocker]]
| + | |
- | [[Category: Scorpion]]
| + | |
- | [[Category: Toxin]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:43:24 2008''
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4] [5] [6] [7]
Publication Abstract from PubMed
Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1 (Kd = 37 nM), Kv1.2 (Kd = 0.8 nM), Kv1.3 (Kd = 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activated potassium channels. It has a unique disulfide pairing among the scorpion toxins family. The solution structure of MTX has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a bended helix from residues 6 to 16 connected by a loop to a two-stranded antiparallel beta sheet (residues 23 to 26 and 28 to 31). The interaction of MTX with the pore region of the Kv1.2 potassium channel has been modeled according to their charge anisotropy. The structure of MTX is similar to other short scorpion toxins despite its peculiar disulfide pairing. Its interaction with the Kv1.2 channel involves a dipole moment, which guides and orients the toxin onto the pore, toward the binding site, and which thus is responsible for the specificity.
Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels.,Blanc E, Sabatier JM, Kharrat R, Meunier S, el Ayeb M, Van Rietschoten J, Darbon H Proteins. 1997 Nov;29(3):321-33. PMID:9365987[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Carlier E, Avdonin V, Geib S, Fajloun Z, Kharrat R, Rochat H, Sabatier JM, Hoshi T, De Waard M. Effect of maurotoxin, a four disulfide-bridged toxin from the chactoid scorpion Scorpio maurus, on Shaker K+ channels. J Pept Res. 2000 Jun;55(6):419-27. PMID:10888198
- ↑ Avdonin V, Nolan B, Sabatier JM, De Waard M, Hoshi T. Mechanisms of maurotoxin action on Shaker potassium channels. Biophys J. 2000 Aug;79(2):776-87. PMID:10920011 doi:http://dx.doi.org/10.1016/S0006-3495(00)76335-1
- ↑ Castle NA, London DO, Creech C, Fajloun Z, Stocker JW, Sabatier JM. Maurotoxin: a potent inhibitor of intermediate conductance Ca2+-activated potassium channels. Mol Pharmacol. 2003 Feb;63(2):409-18. PMID:12527813
- ↑ Regaya I, Beeton C, Ferrat G, Andreotti N, Darbon H, De Waard M, Sabatier JM. Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins. J Biol Chem. 2004 Dec 31;279(53):55690-6. Epub 2004 Oct 21. PMID:15498765 doi:M410055200
- ↑ Pimentel C, M'Barek S, Visan V, Grissmer S, Sampieri F, Sabatier JM, Darbon H, Fajloun Z. Chemical synthesis and 1H-NMR 3D structure determination of AgTx2-MTX chimera, a new potential blocker for Kv1.2 channel, derived from MTX and AgTx2 scorpion toxins. Protein Sci. 2008 Jan;17(1):107-18. Epub 2007 Nov 27. PMID:18042681 doi:ps.073122908
- ↑ Kharrat R, Mabrouk K, Crest M, Darbon H, Oughideni R, Martin-Eauclaire MF, Jacquet G, el Ayeb M, Van Rietschoten J, Rochat H, Sabatier JM. Chemical synthesis and characterization of maurotoxin, a short scorpion toxin with four disulfide bridges that acts on K+ channels. Eur J Biochem. 1996 Dec 15;242(3):491-8. PMID:9022673
- ↑ Kharrat R, Mansuelle P, Sampieri F, Crest M, Oughideni R, Van Rietschoten J, Martin-Eauclaire MF, Rochat H, El Ayeb M. Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: purification, structure and action on potassium channels. FEBS Lett. 1997 Apr 14;406(3):284-90. PMID:9136903
- ↑ Blanc E, Sabatier JM, Kharrat R, Meunier S, el Ayeb M, Van Rietschoten J, Darbon H. Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels. Proteins. 1997 Nov;29(3):321-33. PMID:9365987
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