2jni

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[[Image:2jni.png|left|200px]]
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==Spatial structure of antimicrobial peptide arenicin-2 in aqueous solution==
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<StructureSection load='2jni' size='340' side='right' caption='[[2jni]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2jni]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arenicola_marina Arenicola marina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JNI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JNI FirstGlance]. <br>
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</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=2jni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jni OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jni RCSB], [http://www.ebi.ac.uk/pdbsum/2jni PDBsum]</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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Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged beta-hairpin, formed by two antiparallel beta-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the beta-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells.
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{{STRUCTURE_2jni| PDB=2jni | SCENE= }}
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Recombinant expression, synthesis, purification, and solution structure of arenicin.,Ovchinnikova TV, Shenkarev ZO, Nadezhdin KD, Balandin SV, Zhmak MN, Kudelina IA, Finkina EI, Kokryakov VN, Arseniev AS Biochem Biophys Res Commun. 2007 Aug 17;360(1):156-62. Epub 2007 Jun 14. PMID:17585874<ref>PMID:17585874</ref>
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===Spatial structure of antimicrobial peptide arenicin-2 in aqueous solution===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_17585874}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2jni]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arenicola_marina Arenicola marina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JNI OCA].
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</StructureSection>
[[Category: Arenicola marina]]
[[Category: Arenicola marina]]
[[Category: Arseniev, A S.]]
[[Category: Arseniev, A S.]]

Revision as of 15:35, 12 October 2014

Spatial structure of antimicrobial peptide arenicin-2 in aqueous solution

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