View source for 5zvf


==Structure of [T9,K7]indolicidin, a non glycosylated analogue of indolicidin==
<StructureSection load='5zvf' size='340' side='right'caption='[[5zvf]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zvf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZVF 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=5zvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zvf OCA], [https://pdbe.org/5zvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zvf RCSB], [https://www.ebi.ac.uk/pdbsum/5zvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zvf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CTHL4_BOVIN CTHL4_BOVIN] Potent microbicidal activity; active against S.aureus and E.coli.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Indolicidin is a member of cathelicidin family which displays broad spectrum antimicrobial activity. Severe toxicity and aggregation propensity associated with indolicidin pose a huge limitation to its probable therapeutic application. We are reporting the use of glycosylation strategy to design an analogue of indolicidin and subsequently explore structural and functional effects of sugar on it. Our study led to the design of a potent antibacterial glycosylated peptide, [betaGlc-T9,K7]indolicidin, which showed decreased toxicity against erythrocytes and macrophage cells and thus a higher therapeutic selectivity. The incorporation of sugar also increased the solubility of the peptide. The mode of bacterial killing, functional stability, LPS binding, and cytokine inhibitory potential of the peptide, however, seemed unaffected upon glycosylation. Absence of significant changes in structure upon glycosylation accounts for the possibly retained functions and mode of action of the peptide. Our report thus presents the designing of an indolicidin analogue with improved therapeutic potential by substituting aromatic amino acid with glycosylated amino acid as a promising strategy for the first time.

Design of therapeutically improved analogue of the antimicrobial peptide, indolicidin, using a glycosylation strategy.,Dwivedi R, Aggarwal P, Bhavesh NS, Kaur KJ Amino Acids. 2019 Nov;51(10-12):1443-1460. doi: 10.1007/s00726-019-02779-2. Epub , 2019 Sep 4. PMID:31485742<ref>PMID:31485742</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zvf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Aggarwal P]]
[[Category: Bhavesh NS]]
[[Category: Dwivedi R]]
[[Category: Kaur KJ]]