2i1e

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(New page: 200px<br /><applet load="2i1e" size="350" color="white" frame="true" align="right" spinBox="true" caption="2i1e" /> '''DPC micelle-bound NMR structures of Tritrp2'...)
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[[Image:2i1e.gif|left|200px]]<br /><applet load="2i1e" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2i1e" />
 
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'''DPC micelle-bound NMR structures of Tritrp2'''<br />
 
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==Overview==
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==DPC micelle-bound NMR structures of Tritrp2==
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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.
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<StructureSection load='2i1e' size='340' side='right'caption='[[2i1e]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2i1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I1E FirstGlance]. <br>
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</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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1e OCA], [https://pdbe.org/2i1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i1e RCSB], [https://www.ebi.ac.uk/pdbsum/2i1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i1e ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:16997878</ref>
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2I1E is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1E OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16997878 16997878]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2i1e" style="background-color:#fffaf0;"></div>
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[[Category: Nguyen, L.T.]]
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== References ==
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[[Category: Schibli, D.J.]]
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<references/>
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[[Category: NH2]]
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__TOC__
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[[Category: turn; antimicrobial peptide; micelle-bound peptide]]
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</StructureSection>
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[[Category: Large Structures]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:32:51 2008''
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[[Category: Synthetic construct]]
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[[Category: Nguyen LT]]
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[[Category: Schibli DJ]]

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DPC micelle-bound NMR structures of Tritrp2

PDB ID 2i1e

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