1txm

From Proteopedia

(Difference between revisions)

Current revision

SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAURUS, NMR, 35 STRUCTURES

Structural highlights

1txm is a 1 chain structure with sequence from Scorpio maurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 35 models
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <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>
-</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+</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>
 <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>

1txm

From Proteopedia

Current revision

SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAURUS, NMR, 35 STRUCTURES

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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