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| | ==solution structure of BmKalphaTx11 (major conformation)== | | ==solution structure of BmKalphaTx11 (major conformation)== |
| - | <StructureSection load='2kbh' size='340' side='right' caption='[[2kbh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kbh' size='340' side='right'caption='[[2kbh]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KBH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kbh]] 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=2KBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KBH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kbj|2kbj]], [[2kbk|2kbk]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kbh OCA], [http://pdbe.org/2kbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kbh RCSB], [http://www.ebi.ac.uk/pdbsum/2kbh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kbh ProSAT]</span></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=2kbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kbh OCA], [https://pdbe.org/2kbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kbh RCSB], [https://www.ebi.ac.uk/pdbsum/2kbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kbh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SC11_MESMA SC11_MESMA]] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission (By similarity). Shows analgesic activity when intraperitoneally injected into mice.<ref>PMID:22295565</ref> <ref>PMID:21189156</ref> | + | [https://www.uniprot.org/uniprot/SC11_MESMA SC11_MESMA] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission (By similarity). Shows analgesic activity when intraperitoneally injected into mice.<ref>PMID:22295565</ref> <ref>PMID:21189156</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/2kbh_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/2kbh_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mesobuthus martensii]] | | [[Category: Mesobuthus martensii]] |
| - | [[Category: Wu, H]] | + | [[Category: Wu H]] |
| - | [[Category: Zhu, J]] | + | [[Category: Zhu J]] |
| - | [[Category: Ionic channel inhibitor]]
| + | |
| - | [[Category: Neurotoxin]]
| + | |
| - | [[Category: Protein]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Sodium channel inhibitor]]
| + | |
| - | [[Category: Toxin]]
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| Structural highlights
Function
SC11_MESMA Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission (By similarity). Shows analgesic activity when intraperitoneally injected into mice.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The solution structure of BmKalphaTx11 presented by this paper is distinctive from any other structures of wide-type scorpion alpha-toxins reported so far, for its trans-9,10 peptide bond conformation is accompanied by 'protruding' topology of the 'NC-domain'. The orientation of the C-tail of BmKalphaTx11 is obviously different from that of classical alpha-toxins (e.g., AaH2, BmK-M8), despite the fact that they share common trans conformation of peptide bond between residues 9 and 10. Accordingly, there must be other structural factors dominating the orientation of the C-tail except the conformation of peptide bond 9-10. Our study reveals that residues at position 58 play an important role in it, and different type of residues at this position (e.g., Lys, Arg, Met, Ile) result in different spatial relationship between the C-terminus and the 'five-residue-turn' and then different topology of the 'NC-domain', therefore residues at position 58 are believed to function as structure and bioactivity switch for specificity of scorpion alpha-toxins. The mechanism for stabilizing the geometry of the 'NC-domain' in wide-type scorpion alpha-toxins is also discussed.
Solution structure of BmKalphaTx11, a toxin from the venom of the Chinese scorpion Buthus martensii Karsch.,Zhu J, Tong X, Cao C, Wu G, Zhang N, Wu H Biochem Biophys Res Commun. 2010 Jan 1;391(1):627-33. Epub 2009 Nov 22. PMID:19932686[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang R, Yang Z, Liu YF, Cui Y, Zhang JH. Purification, characterization and cDNA cloning of an analgesic peptide from the Chinese scorpion Buthus martensii Karsch (BmK AGP-SYPU2). Mol Biol (Mosk). 2011 Nov-Dec;45(6):956-62. PMID:22295565
- ↑ Zhang R, Cui Y, Zhang X, Yang Z, Zhao Y, Song Y, Wu C, Zhang J. Soluble expression, purification and the role of C-terminal glycine residues in scorpion toxin BmK AGP-SYPU2. BMB Rep. 2010 Dec;43(12):801-6. doi: 10.5483/BMBRep.2010.43.12.801. PMID:21189156 doi:http://dx.doi.org/10.5483/BMBRep.2010.43.12.801
- ↑ Zhu J, Tong X, Cao C, Wu G, Zhang N, Wu H. Solution structure of BmKalphaTx11, a toxin from the venom of the Chinese scorpion Buthus martensii Karsch. Biochem Biophys Res Commun. 2010 Jan 1;391(1):627-33. Epub 2009 Nov 22. PMID:19932686 doi:10.1016/j.bbrc.2009.11.110
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