8aoo
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8aoo is ON HOLD Authors: Personne, H., Stocker, A., Reymond, J.-L. Description: Fucosylated mixed-chirality linear peptide HP055 bound to the fucos...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Fucosylated mixed-chirality linear peptide FHP31 bound to the fucose binding lectin LecB PA-IIL from Pseudomonas aeruginosa at 1.2 Angstrom resolution.== | |
| + | <StructureSection load='8aoo' size='340' side='right'caption='[[8aoo]], [[Resolution|resolution]] 1.18Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8aoo]] is a 8 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=8AOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AOO 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]] 1.18Å</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=8aoo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aoo OCA], [https://pdbe.org/8aoo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aoo RCSB], [https://www.ebi.ac.uk/pdbsum/8aoo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aoo 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Personne | + | <div class="pdbe-citations 8aoo" style="background-color:#fffaf0;"></div> |
| - | [[Category: Reymond | + | == References == |
| - | [[Category: Stocker | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa PAO1]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Personne H]] | ||
| + | [[Category: Reymond J-L]] | ||
| + | [[Category: Stocker A]] | ||
Current revision
Fucosylated mixed-chirality linear peptide FHP31 bound to the fucose binding lectin LecB PA-IIL from Pseudomonas aeruginosa at 1.2 Angstrom resolution.
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