2n8d
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2n8d is ON HOLD Authors: Pillong, M., Blatter, M., Schneider, G. Description: In silico designed antimicrobial peptide Lavracin [[Category: Unrelea...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==In silico designed antimicrobial peptide Lavracin== | |
| + | <StructureSection load='2n8d' size='340' side='right'caption='[[2n8d]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n8d]] 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2n8d" style="background-color:#fffaf0;"></div> |
| - | [[Category: Blatter | + | == References == |
| - | [[Category: Schneider | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Blatter M]] | ||
| + | [[Category: Pillong M]] | ||
| + | [[Category: Schneider G]] | ||
Current revision
In silico designed antimicrobial peptide Lavracin
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