2bmt
From Proteopedia
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| - | [[Image:2bmt.jpg|left|200px]]<br /><applet load="2bmt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2bmt" /> | ||
| - | '''SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES'''<br /> | ||
| - | == | + | ==SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES== |
| + | <StructureSection load='2bmt' size='340' side='right'caption='[[2bmt]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2bmt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BMT FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=2bmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmt OCA], [https://pdbe.org/2bmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bmt RCSB], [https://www.ebi.ac.uk/pdbsum/2bmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bmt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KAX16_MESMA KAX16_MESMA] Potent blocker of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1.3/KCNA3 (PubMed:9354615) and ERG1/Kv11.1/KCNH2 (PubMed:18687312)). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The solution structure of BmTX2 purified from the venom of the Chinese Buthid Buthus martensi has been determined by 2D NMR spectroscopy techniques which led to the description of its 3D conformation. The structure consists of a triple-stranded beta-sheet connected to a helical structure. This helix encompasses 10 residues, from 11 to 20, begins with a turn of 310 helix, and ends with an alpha helix. The three strands of beta sheet comprise residues 2-6, with a bulge covering residues 4 and 5, 26-29, and 32-35, with a type I' beta turn centered on residues 30-31. We also characterized the solution structure of BmTX1. The two toxins which are potent blockers of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1. 3) are highly superimposable and possess the same structural characteristics. Analysis of these structures allows us to hypothesize that, besides the main surface of interaction described by the functional map of charybdotoxin, one can expect that the binding of scorpion toxins on BKCa channels may involve residues on the edge of this surface. | The solution structure of BmTX2 purified from the venom of the Chinese Buthid Buthus martensi has been determined by 2D NMR spectroscopy techniques which led to the description of its 3D conformation. The structure consists of a triple-stranded beta-sheet connected to a helical structure. This helix encompasses 10 residues, from 11 to 20, begins with a turn of 310 helix, and ends with an alpha helix. The three strands of beta sheet comprise residues 2-6, with a bulge covering residues 4 and 5, 26-29, and 32-35, with a type I' beta turn centered on residues 30-31. We also characterized the solution structure of BmTX1. The two toxins which are potent blockers of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1. 3) are highly superimposable and possess the same structural characteristics. Analysis of these structures allows us to hypothesize that, besides the main surface of interaction described by the functional map of charybdotoxin, one can expect that the binding of scorpion toxins on BKCa channels may involve residues on the edge of this surface. | ||
| - | + | Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels.,Blanc E, Romi-Lebrun R, Bornet O, Nakajima T, Darbon H Biochemistry. 1998 Sep 8;37(36):12412-8. PMID:9730813<ref>PMID:9730813</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2bmt" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mesobuthus martensii]] | ||
| + | [[Category: Blanc E]] | ||
| + | [[Category: Bornet O]] | ||
| + | [[Category: Darbon H]] | ||
| + | [[Category: Nakajima T]] | ||
| + | [[Category: Romi-Lebrun R]] | ||
Current revision
SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES
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