View source for 5lcs


==NMR structure of Chicken AvBD7 defensin==
<StructureSection load='5lcs' size='340' side='right'caption='[[5lcs]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lcs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LCS FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=5lcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcs OCA], [https://pdbe.org/5lcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lcs RCSB], [https://www.ebi.ac.uk/pdbsum/5lcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLL7_CHICK GLL7_CHICK] Has bactericidal activity.
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== Publication Abstract from PubMed ==
Defensins are frontline peptides of mucosal immunity in the animal kingdom, including birds. Their resistance to proteolysis and their ensuing ability to maintain antimicrobial potential remains questionable and was therefore investigated. We have shown by bottom-up mass spectrometry analysis of protein extracts that both avian beta-defensins AvBD2 and AvBD7 were ubiquitously distributed along the chicken gut. Cathepsin B was found by immunoblotting in jejunum, ileum, caecum, and caecal tonsils, while cathepsins K, L, and S were merely identified in caecal tonsils. Hydrolysis product of AvBD2 and AvBD7 incubated with a panel of proteases was analysed by RP-HPLC, mass spectrometry and antimicrobial assays. AvBD2 and AvBD7 were resistant to serine proteases and to cathepsins D and H. Conversely cysteine cathepsins B, K, L, and S degraded AvBD2 and abolished its antibacterial activity. Only cathepsin K cleaved AvBD7 and released Ile4-AvBD7, a N-terminal truncated natural peptidoform of AvBD7 that displayed antibacterial activity. Besides the 3-stranded antiparallel beta-sheet typical of beta-defensins, structural analysis of AvBD7 by two-dimensional NMR spectroscopy highlighted the restricted accessibility of the C-terminus embedded by the N-terminal region and gave a formal evidence of a salt bridge (Asp9-Arg12) that could account for proteolysis resistance. The differential susceptibility of avian defensins to proteolysis opens intriguing questions about a distinctive role in the mucosal immunity against pathogen invasion.

The Unusual Resistance of Avian Defensin AvBD7 to Proteolytic Enzymes Preserves Its Antibacterial Activity.,Bailleul G, Kravtzoff A, Joulin-Giet A, Lecaille F, Labas V, Meudal H, Loth K, Teixeira-Gomes AP, Gilbert FB, Coquet L, Jouenne T, Bromme D, Schouler C, Landon C, Lalmanach G, Lalmanach AC PLoS One. 2016 Aug 25;11(8):e0161573. doi: 10.1371/journal.pone.0161573., eCollection 2016. PMID:27561012<ref>PMID:27561012</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lcs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Landon C]]
[[Category: Loth K]]
[[Category: Meudal H]]