5v1e

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'''Unreleased structure'''
 
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The entry 5v1e is ON HOLD
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==Suboptimization of a glycine rich peptide allows the combinatorial space exploration for designing novel antimicrobial peptides==
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<StructureSection load='5v1e' size='340' side='right'caption='[[5v1e]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5v1e]] 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=5V1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V1E 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, 10 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=5v1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1e OCA], [https://pdbe.org/5v1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v1e RCSB], [https://www.ebi.ac.uk/pdbsum/5v1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1e 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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Plants are extensively used in traditional medicine, and several plant antimicrobial peptides have been described as potential alternatives to conventional antibiotics. However, after more than four decades of research no plant antimicrobial peptide is currently used for treating bacterial infections, due to their length, post-translational modifications or high dose requirement for a therapeutic effect . Here we report the design of antimicrobial peptides derived from a guava glycine-rich peptide using a genetic algorithm. This approach yields guavanin peptides, arginine-rich alpha-helical peptides that possess an unusual hydrophobic counterpart mainly composed of tyrosine residues. Guavanin 2 is characterized as a prototype peptide in terms of structure and activity. Nuclear magnetic resonance analysis indicates that the peptide adopts an alpha-helical structure in hydrophobic environments. Guavanin 2 is bactericidal at low concentrations, causing membrane disruption and triggering hyperpolarization. This computational approach for the exploration of natural products could be used to design effective peptide antibiotics.
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Authors:
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In silico optimization of a guava antimicrobial peptide enables combinatorial exploration for peptide design.,Porto WF, Irazazabal L, Alves ESF, Ribeiro SM, Matos CO, Pires AS, Fensterseifer ICM, Miranda VJ, Haney EF, Humblot V, Torres MDT, Hancock REW, Liao LM, Ladram A, Lu TK, de la Fuente-Nunez C, Franco OL Nat Commun. 2018 Apr 16;9(1):1490. doi: 10.1038/s41467-018-03746-3. PMID:29662055<ref>PMID:29662055</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5v1e" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Alves ESF]]
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[[Category: Matos CO]]

Current revision

Suboptimization of a glycine rich peptide allows the combinatorial space exploration for designing novel antimicrobial peptides

PDB ID 5v1e

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