5m9u
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Spatial structure of antimicrobial peptide arenicin-1 mutant V8R== | |
| + | <StructureSection load='5m9u' size='340' side='right'caption='[[5m9u]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arenicola_marina Arenicola marina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M9U 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5m9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9u OCA], [https://pdbe.org/5m9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m9u RCSB], [https://www.ebi.ac.uk/pdbsum/5m9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANN1_AREMA ANN1_AREMA] Has antimicrobial activity against the Gram-negative bacteria E.coli and P.mirabilis, the Gram-positive bacterium L.monocytogenes and the yeast C.albicans.<ref>PMID:15527787</ref> <ref>PMID:17935487</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The beta-hairpin antimicrobial peptides arenicins from marine polychaeta Arenicola marina exhibit a broad spectrum of antimicrobial activity and high cytotoxicity. In this study the biological activities of arenicin-1 and its therapeutically valuable analog Ar-1[V8R] were investigated. The peptide Ar-1[V8R] displays significantly reduced cytotoxicity against mammalian cells relative to the wild-type arenicin-1. At the same time, both peptides exhibit similar antibacterial activities and kinetics of bacterial membrane permeabilization. Comparative NMR analysis of the peptides spatial structures in water and membrane-mimicking environment showed that Ar-1[V8R] in contrast to arenicin has significantly lower dimerization propensity. Thus, dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity. | ||
| - | + | Dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity.,Panteleev PV, Myshkin MY, Shenkarev ZO, Ovchinnikova TV Biochem Biophys Res Commun. 2017 Jan 22;482(4):1320-1326. doi:, 10.1016/j.bbrc.2016.12.035. Epub 2016 Dec 8. PMID:27940358<ref>PMID:27940358</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Myshkin | + | <div class="pdbe-citations 5m9u" style="background-color:#fffaf0;"></div> |
| - | [[Category: Ovchinnikova | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Arenicola marina]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Myshkin MY]] | ||
| + | [[Category: Ovchinnikova TV]] | ||
| + | [[Category: Panteleev PV]] | ||
| + | [[Category: Shenkarev ZO]] | ||
Current revision
Spatial structure of antimicrobial peptide arenicin-1 mutant V8R
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