View source for 8anr


==Fucosylated alternate chirality linear peptide FHP30 bound to the fucose binding lectin LecB PA-IIL from Pseudomonas aeruginosa at 1.6 Angstrom resolution.==
<StructureSection load='8anr' size='340' side='right'caption='[[8anr]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8anr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ANR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ANR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DLY:D-LYSINE'>DLY</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ZDC:3,7-ANHYDRO-2,8-DIDEOXY-L-GLYCERO-D-GLUCO-OCTONIC+ACID'>ZDC</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=8anr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8anr OCA], [https://pdbe.org/8anr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8anr RCSB], [https://www.ebi.ac.uk/pdbsum/8anr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8anr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9HYN5_PSEAE Q9HYN5_PSEAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Membrane disruptive alpha-helical antimicrobial peptides (AMPs) offer an opportunity to address multidrug resistance; however, most AMPs are toxic and unstable in serum. These limitations can be partly overcome by introducing D-residues, which often confers protease resistance and reduces toxicity without affecting antibacterial activity, presumably due to lowered alpha-helicity. Here, we investigated 31 diastereomers of the alpha-helical AMP KKLLKLLKLLL. Three diastereomers containing two, three, and four D-residues showed increased antibacterial effects, comparable hemolysis, reduced toxicity against HEK293 cells, and excellent serum stability, while another diastereomer with four D-residues additionally displayed lower hemolysis. X-ray crystallography confirmed that high or low alpha-helicity as measured by circular dichroism indicated alpha-helical or disordered structures independently of the number of chirality switched residues. In contrast to previous reports, alpha-helicity across diastereomers correlated with both antibacterial activity and hemolysis and revealed a complex relationship between stereochemistry, activity, and toxicity, highlighting the potential of diastereomers for property optimization.

To Fold or Not to Fold: Diastereomeric Optimization of an alpha-Helical Antimicrobial Peptide.,Personne H, Paschoud T, Fulgencio S, Baeriswyl S, Kohler T, van Delden C, Stocker A, Javor S, Reymond JL J Med Chem. 2023 Jun 8;66(11):7570-7583. doi: 10.1021/acs.jmedchem.3c00460. Epub , 2023 May 25. PMID:37227046<ref>PMID:37227046</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8anr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Synthetic construct]]
[[Category: Personne H]]
[[Category: Reymond J-L]]
[[Category: Stocker A]]