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| ==In silico designed antimicrobial peptide Lavracin== | | ==In silico designed antimicrobial peptide Lavracin== |
| <StructureSection load='2n8d' size='340' side='right'caption='[[2n8d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='2n8d' size='340' side='right'caption='[[2n8d]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2n8d]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N8D FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N8D 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n8d OCA], [https://pdbe.org/2n8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n8d RCSB], [https://www.ebi.ac.uk/pdbsum/2n8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n8d 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=2n8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n8d OCA], [https://pdbe.org/2n8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n8d RCSB], [https://www.ebi.ac.uk/pdbsum/2n8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n8d ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Specific interactions of peptides with lipid membranes are essential for cellular communication and constitute a central aspect of the innate host defense against pathogens. A computational method for generating innovative membrane-pore-forming peptides inspired by natural templates is presented. Peptide representation in terms of sequence- and topology-dependent hydrophobic moments is introduced. This design concept proves to be appropriate for the de novo generation of first-in-class membrane-active peptides with the anticipated mode of action. The designed peptides outperform the natural template in terms of their antibacterial activity. They form a kinked helical structure and self-assemble in the membrane by an entropy-driven mechanism to form dynamically growing pores that are dependent on the lipid composition. The results of this study demonstrate the unique potential of natural template-based peptide design for chemical biology and medicinal chemistry.
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| Rational Design of Membrane-Pore-Forming Peptides.,Pillong M, Hiss JA, Schneider P, Lin YC, Posselt G, Pfeiffer B, Blatter M, Muller AT, Bachler S, Neuhaus CS, Dittrich PS, Altmann KH, Wessler S, Schneider G Small. 2017 Aug 11. doi: 10.1002/smll.201701316. PMID:28799716<ref>PMID:28799716</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2n8d" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Blatter, M]] | | [[Category: Blatter M]] |
| [[Category: Pillong, M]] | | [[Category: Pillong M]] |
| [[Category: Schneider, G]] | | [[Category: Schneider G]] |
| [[Category: Antimicrobial peptide]]
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| [[Category: De novo protein]]
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