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| | ==DPC micelle-bound NMR structures of Tritrp1== | | ==DPC micelle-bound NMR structures of Tritrp1== |
| - | <StructureSection load='2i1d' size='340' side='right' caption='[[2i1d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2i1d' size='340' side='right'caption='[[2i1d]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2i1d]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I1D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2i1d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I1D 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</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2i1e|2i1e]], [[2i1f|2i1f]], [[2i1g|2i1g]], [[2i1h|2i1h]], [[2i1i|2i1i]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2i1d RCSB], [http://www.ebi.ac.uk/pdbsum/2i1d PDBsum]</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=2i1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1d OCA], [https://pdbe.org/2i1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i1d RCSB], [https://www.ebi.ac.uk/pdbsum/2i1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i1d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PF11_PIG PF11_PIG]] Prophenin-1: Exerts antimicrobial activity. It is more effective against Gram-negative bacteria than Gram-positive bacteria.<ref>PMID:16997878</ref> Tritrpticin: Cathelicidin-like peptide with antimicrobial and hemolytic activities.<ref>PMID:16997878</ref> | + | [https://www.uniprot.org/uniprot/PF11_PIG PF11_PIG] Prophenin-1: Exerts antimicrobial activity. It is more effective against Gram-negative bacteria than Gram-positive bacteria.<ref>PMID:16997878</ref> Tritrpticin: Cathelicidin-like peptide with antimicrobial and hemolytic activities.<ref>PMID:16997878</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2i1d" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Nguyen, L T]] | + | [[Category: Large Structures]] |
| - | [[Category: Schibli, D J]] | + | [[Category: Sus scrofa]] |
| - | [[Category: Antimicrobial peptide]] | + | [[Category: Nguyen LT]] |
| - | [[Category: Antimicrobial protein]] | + | [[Category: Schibli DJ]] |
| - | [[Category: Micelle-bound peptide]]
| + | |
| - | [[Category: Turn]]
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| Structural highlights
Function
PF11_PIG Prophenin-1: Exerts antimicrobial activity. It is more effective against Gram-negative bacteria than Gram-positive bacteria.[1] Tritrpticin: Cathelicidin-like peptide with antimicrobial and hemolytic activities.[2]
Publication Abstract from PubMed
Tritrpticin is a member of the cathelicidin family of antimicrobial peptides. Starting from its native sequence (VRRFPWWWPFLRR), eight synthetic peptide analogs were studied to investigate the roles of specific residues in its biological and structural properties. This included amidation of the C-terminus paired with substitutions of its cationic and Phe residues, as well as the Pro residues that are important for its two-turn micelle-bound structure. These analogs were determined to have a significant antimicrobial potency. In contrast, two other peptide analogs, those with the three Trp residues substituted with either Phe or Tyr residues are not highly membrane perturbing, as determined by leakage and flip-flop assays using fluorescence spectroscopy. Nevertheless the Phe analog has a high activity; this suggests an intracellular mechanism for antimicrobial activity that may be part of the overall mechanism of action of native tritrpticin as a complement to membrane perturbation. NMR experiments of these two Trp-substituted peptides showed the presence of multiple conformers. The structures of the six remaining Trp-containing analogs bound to dodecylphosphocholine micelles showed major, well-defined conformations. These peptides are membrane disruptive and show a wide range in hemolytic activity. Their micelle-bound structures either retain the typical turn-turn structure of native tritrpticin or have an extended alpha-helix. This work demonstrates that closely related antimicrobial peptides can often have remarkably altered properties with complex influences on their biological activities.
Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures.,Schibli DJ, Nguyen LT, Kernaghan SD, Rekdal O, Vogel HJ Biophys J. 2006 Dec 15;91(12):4413-26. Epub 2006 Sep 22. PMID:16997878[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schibli DJ, Nguyen LT, Kernaghan SD, Rekdal O, Vogel HJ. Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures. Biophys J. 2006 Dec 15;91(12):4413-26. Epub 2006 Sep 22. PMID:16997878 doi:biophysj.106.085837
- ↑ Schibli DJ, Nguyen LT, Kernaghan SD, Rekdal O, Vogel HJ. Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures. Biophys J. 2006 Dec 15;91(12):4413-26. Epub 2006 Sep 22. PMID:16997878 doi:biophysj.106.085837
- ↑ Schibli DJ, Nguyen LT, Kernaghan SD, Rekdal O, Vogel HJ. Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures. Biophys J. 2006 Dec 15;91(12):4413-26. Epub 2006 Sep 22. PMID:16997878 doi:biophysj.106.085837
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