6y13
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6y13 is ON HOLD Authors: Baeriswyl, S., Stocker, A., Reymond, J.-L. Description: Bicyclic stapled peptide bp94 at 1.1 Angstrom resolution [[Categor...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Bicyclic stapled peptide bp70 at 1.1 Angstrom resolution== | |
| + | <StructureSection load='6y13' size='340' side='right'caption='[[6y13]], [[Resolution|resolution]] 1.11Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6y13]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y13 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAB:2,4-DIAMINOBUTYRIC+ACID'>DAB</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=O65:3,5-bis(hydroxymethyl)-4-methyl-benzaldehyde'>O65</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</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=6y13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y13 OCA], [https://pdbe.org/6y13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y13 RCSB], [https://www.ebi.ac.uk/pdbsum/6y13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y13 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The peptide alpha-helix is right-handed when containing amino acids with l-chirality, and left-handed with d-chirality, however mixed chirality peptides generally do not form alpha-helices unless a helix inducer such as the non-natural residue amino-isobutyric acid is used. Herein we report the first X-ray crystal structures of mixed chirality alpha-helices in short peptides comprising only natural residues as the example of a stapled bicyclic and a linear membrane disruptive amphiphilic antimicrobial peptide (AMP) containing seven l- and four d-residues, as complexes of fucosylated analogs with the bacterial lectin LecB. The mixed chirality alpha-helices are superimposable onto the homochiral alpha-helices and form under similar conditions as shown by CD spectra and MD simulations but non-hemolytic and resistant to proteolysis. The observation of a mixed chirality alpha-helix with only natural residues in the protein environment of LecB suggests a vast unexplored territory of alpha-helical mixed chirality sequences and their possible use for optimizing bioactive alpha-helical peptides. | ||
| - | + | A mixed chirality alpha-helix in a stapled bicyclic and a linear antimicrobial peptide revealed by X-ray crystallography.,Baeriswyl S, Personne H, Di Bonaventura I, Kohler T, van Delden C, Stocker A, Javor S, Reymond JL RSC Chem Biol. 2021 Aug 20;2(6):1608-1617. doi: 10.1039/d1cb00124h. eCollection, 2021 Dec 2. PMID:34977576<ref>PMID:34977576</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6y13" style="background-color:#fffaf0;"></div> |
| - | [[Category: Baeriswyl | + | == References == |
| - | [[Category: Stocker | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Baeriswyl S]] | ||
| + | [[Category: Reymond J-L]] | ||
| + | [[Category: Stocker A]] | ||
Current revision
Bicyclic stapled peptide bp70 at 1.1 Angstrom resolution
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