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| | ==STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES== | | ==STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES== |
| - | <StructureSection load='1bh1' size='340' side='right' caption='[[1bh1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1bh1' size='340' side='right'caption='[[1bh1]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bh1]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bh1]] 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=1BH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BH1 FirstGlance]. <br> |
| - | </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> | + | </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=1bh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh1 OCA], [http://pdbe.org/1bh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1bh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bh1 ProSAT]</span></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=1bh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh1 OCA], [https://pdbe.org/1bh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bh1 RCSB], [https://www.ebi.ac.uk/pdbsum/1bh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bh1 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Barnham, K J]] | + | [[Category: Apis mellifera]] |
| - | [[Category: Bartone, N]] | + | [[Category: Large Structures]] |
| - | [[Category: Curtain, C]] | + | [[Category: Barnham KJ]] |
| - | [[Category: Hewish, D]] | + | [[Category: Bartone N]] |
| - | [[Category: Kirkpatrick, A]] | + | [[Category: Curtain C]] |
| - | [[Category: Liu, S T]] | + | [[Category: Hewish D]] |
| - | [[Category: Norton, R]] | + | [[Category: Kirkpatrick A]] |
| - | [[Category: Rivett, D]] | + | [[Category: Liu ST]] |
| - | [[Category: Werkmeister, J]] | + | [[Category: Norton R]] |
| - | [[Category: Hemolytic polypeptide]]
| + | [[Category: Rivett D]] |
| - | [[Category: Toxin]]
| + | [[Category: Werkmeister J]] |
| 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
D-Pro14 melittin was synthesized to investigate the effect of increasing the angle of the bend in the hinge region between the helical segments of the molecule. Structural analysis by nuclear magnetic resonance indicated that, in methanol, the molecule consisted of two helices separated at Pro14, as in melittin. However, the two helices in D-Pro14 melittin were laterally displaced relative to each other by approximately 7 A, and in addition, there was a small rotation of the carboxyl-terminal helix relative to the amino-terminal helix around the long axis of the molecule. The peptide had less than 5% of the cytolytic activity of melittin. Modification of Arg22 with the 2,2,5,7,8-pentamethyl-chroman-6-sulphonyl (pmc) group restored hemolytic activity to close to that of unmodified melittin. Replacement of Arg22 with Phe was less effective in restoring hemolytic activity. Electron-paramagnetic resonance studies suggest that there is a positive correlation between hemolytic activity of the peptides and interaction with phospholipid bilayers.
Structure and activity of D-Pro14 melittin.,Hewish DR, Barnham KJ, Werkmeister JA, Kirkpatrick A, Bartone N, Liu ST, Norton RS, Curtain C, Rivetta DE J Protein Chem. 2002 May;21(4):243-53. PMID:12168695[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
- ↑ Hewish DR, Barnham KJ, Werkmeister JA, Kirkpatrick A, Bartone N, Liu ST, Norton RS, Curtain C, Rivetta DE. Structure and activity of D-Pro14 melittin. J Protein Chem. 2002 May;21(4):243-53. PMID:12168695
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