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| | ==Spatial structure of antimicrobial peptide arenicin-1 mutant V8R== | | ==Spatial structure of antimicrobial peptide arenicin-1 mutant V8R== |
| - | <StructureSection load='5m9u' size='340' side='right'caption='[[5m9u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5m9u' size='340' side='right'caption='[[5m9u]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5m9u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arema Arema]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M9U FirstGlance]. <br> | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9u OCA], [http://pdbe.org/5m9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m9u RCSB], [http://www.ebi.ac.uk/pdbsum/5m9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9u ProSAT]</span></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=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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arema]] | + | [[Category: Arenicola marina]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myshkin, M Y]] | + | [[Category: Myshkin MY]] |
| - | [[Category: Ovchinnikova, T V]] | + | [[Category: Ovchinnikova TV]] |
| - | [[Category: Panteleev, P V]] | + | [[Category: Panteleev PV]] |
| - | [[Category: Shenkarev, Z O]] | + | [[Category: Shenkarev ZO]] |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Structure from cyana 3 97]]
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| Structural highlights
Function
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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ovchinnikova TV, Aleshina GM, Balandin SV, Krasnosdembskaya AD, Markelov ML, Frolova EI, Leonova YF, Tagaev AA, Krasnodembsky EG, Kokryakov VN. Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina. FEBS Lett. 2004 Nov 5;577(1-2):209-14. PMID:15527787 doi:http://dx.doi.org/10.1016/j.febslet.2004.10.012
- ↑ Andra J, Jakovkin I, Grotzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M. Structure and mode of action of the antimicrobial peptide arenicin. Biochem J. 2008 Feb 15;410(1):113-22. PMID:17935487 doi:http://dx.doi.org/BJ20071051
- ↑ Panteleev PV, Myshkin MY, Shenkarev ZO, Ovchinnikova TV. Dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2016.12.035
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