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| | ==Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue== | | ==Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue== |
| - | <StructureSection load='2mw6' size='340' side='right'caption='[[2mw6]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2mw6' size='340' side='right'caption='[[2mw6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mw6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MW6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mw6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MW6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3UQ:[(1,2,3,4,5-ETA)-CYCLOPENTADIENYL][(1,2,3,4,4A,8A-ETA)-NAPHTHALENE]RUTHENIUM(1+)'>3UQ</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3UQ:[(1,2,3,4,5-ETA)-CYCLOPENTADIENYL][(1,2,3,4,4A,8A-ETA)-NAPHTHALENE]RUTHENIUM(1+)'>3UQ</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mlt|2mlt]]</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=2mw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mw6 OCA], [https://pdbe.org/2mw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mw6 RCSB], [https://www.ebi.ac.uk/pdbsum/2mw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mw6 ProSAT]</span></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=2mw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mw6 OCA], [http://pdbe.org/2mw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mw6 RCSB], [http://www.ebi.ac.uk/pdbsum/2mw6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mw6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MEL_APIME MEL_APIME]] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref> Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref> | + | [https://www.uniprot.org/uniprot/MEL_APIME MEL_APIME] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref> Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Apis mellifera]] | | [[Category: Apis mellifera]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Novikov, V V]] | + | [[Category: Novikov VV]] |
| - | [[Category: Pavlov, A A]] | + | [[Category: Pavlov AA]] |
| - | [[Category: Perekalin, D S]] | + | [[Category: Perekalin DS]] |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
MEL_APIME Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.[1] Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.[2]
Publication Abstract from PubMed
Melittin is a membrane-active peptide from bee venom with promising antimicrobial and anticancer activity. Herein we report on a simple and selective method for labeling of the tryptophan residue in melittin by the organometallic fragment [(C5 H5 )Ru](+) in aqueous solution and in air. Ruthenium coordination does not disturb the secondary structure of the peptide (as verified by 2D NMR spectroscopy), but changes the pattern of its intermolecular interactions resulting in an 11-fold decrease of hemolytic activity. The high stability of the organometallic conjugate allowed the establishment of the biodistribution of the labeled melittin in mice by inductively coupled plasma MS analysis of ruthenium.
Selective ruthenium labeling of the tryptophan residue in the bee venom Peptide melittin.,Perekalin DS, Novikov VV, Pavlov AA, Ivanov IA, Anisimova NY, Kopylov AN, Volkov DS, Seregina IF, Bolshov MA, Kudinov AR Chemistry. 2015 Mar 23;21(13):4923-5. doi: 10.1002/chem.201406510. Epub 2015 Feb , 16. PMID:25688543[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sciani JM, Marques-Porto R, Lourenco Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC. Identification of a novel melittin isoform from Africanized Apis mellifera venom. Peptides. 2010 Aug;31(8):1473-9. doi: 10.1016/j.peptides.2010.05.001. Epub 2010, May 21. PMID:20472009 doi:http://dx.doi.org/10.1016/j.peptides.2010.05.001
- ↑ Sciani JM, Marques-Porto R, Lourenco Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC. Identification of a novel melittin isoform from Africanized Apis mellifera venom. Peptides. 2010 Aug;31(8):1473-9. doi: 10.1016/j.peptides.2010.05.001. Epub 2010, May 21. PMID:20472009 doi:http://dx.doi.org/10.1016/j.peptides.2010.05.001
- ↑ Perekalin DS, Novikov VV, Pavlov AA, Ivanov IA, Anisimova NY, Kopylov AN, Volkov DS, Seregina IF, Bolshov MA, Kudinov AR. Selective ruthenium labeling of the tryptophan residue in the bee venom Peptide melittin. Chemistry. 2015 Mar 23;21(13):4923-5. doi: 10.1002/chem.201406510. Epub 2015 Feb , 16. PMID:25688543 doi:http://dx.doi.org/10.1002/chem.201406510
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