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==Identification of the Structural Traits Mediating the Antimicrobial Activity of a Chimeric Peptide of HBD2 and HBD3==
<StructureSection load='2lxo' size='340' side='right'caption='[[2lxo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lxo]] 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=2LXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LXO 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=2lxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxo OCA], [https://pdbe.org/2lxo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lxo RCSB], [https://www.ebi.ac.uk/pdbsum/2lxo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxo ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antimicrobial peptides participate in the first line of defence of many organisms against pathogens. In humans, the family of beta-defensins plays a pivotal role in innate immunity. Two human beta-defensins, beta-defensin-2 and -3 (HBD2 and HBD3), show substantial sequence identity and structural similarity. However, HBD3 kills Staphylococcus (S.) aureus with a 4- to 8-fold higher efficiency compared to HBD2, whereas their activities against Escherichia (E.) coli are very similar. The generation of six HBD2/HBD3-chimeric molecules led to the identification of distinct molecular regions which mediate their divergent killing properties. One of the chimeras (chimera C3) killed both E. coli and S. aureus with an even higher efficacy compared to the wild-type molecules. Due to the broad spectrum of its antimicrobial activity against many human multidrug-resistant pathogens, this HBD2/HBD3-chimeric peptide represents a promising candidate for a new class of antibiotics. In order to investigate the structural basis of its exceptional antimicrobial activity, the peptide's tertiary structure was determined by NMR spectroscopy, which allowed its direct comparison to the published structures of HBD2 and HBD3 and the identification of the activity-increasing molecular features.

Identification of structural traits that increase the antimicrobial activity of a chimeric peptide of human beta-defensins 2 and 3.,Spudy B, Sonnichsen FD, Waetzig GH, Grotzinger J, Jung S Biochem Biophys Res Commun. 2012 Oct 12;427(1):207-11. doi:, 10.1016/j.bbrc.2012.09.052. Epub 2012 Sep 18. PMID:22995312<ref>PMID:22995312</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Grotzinger J]]
[[Category: Jung S]]
[[Category: Soennichsen FD]]
[[Category: Spudy B]]
[[Category: Waetzig GH]]