2lr5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==1H chemical shift assignments for micasin== | |
| + | <StructureSection load='2lr5' size='340' side='right'caption='[[2lr5]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lr5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microsporum_canis Microsporum canis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LR5 FirstGlance]. <br> | ||
| + | </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=2lr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lr5 OCA], [https://pdbe.org/2lr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lr5 RCSB], [https://www.ebi.ac.uk/pdbsum/2lr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lr5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fungi are a newly emerging source of peptide antibiotics with therapeutic potential. Here, we report 17 new fungal defensin-like peptide (fDLP) genes and the detailed characterization of a corresponding synthetic fDLP (micasin) from a dermatophyte in terms of its structure, activity and therapeutic potential. NMR analysis showed that synthetic micasin adopts a "hallmark" cysteine-stablized alpha-helical and beta-sheet fold. It was active on both Gram-positive and Gram-negtive bacteria, and importantly it killed two clinical isolates of methicillin-resistant Staphylococcus aureus and the opportunistic pathogen Pseudomonas aeruginosa at low micromolar concentrations. Micasin killed approximately 100% of treated bacteria within 3 h through a membrane nondisruptive mechanism of action, and showed extremely low hemolysis and high serum stability. Consistent with these functional properties, micasin increases survival in mice infected by the pathogenic bacteria in a peritonitis model. Our work represents a valuable approach to explore novel peptide antibiotics from a large resource of fungal genomes. | ||
| - | + | Dermatophytic defensin with antiinfective potential.,Zhu S, Gao B, Harvey PJ, Craik DJ Proc Natl Acad Sci U S A. 2012 May 29;109(22):8495-500. Epub 2012 May 14. PMID:22586077<ref>PMID:22586077</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2lr5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Microsporum canis]] | ||
| + | [[Category: Craik DJ]] | ||
| + | [[Category: Harvey PJ]] | ||
| + | [[Category: Zhu S]] | ||
Current revision
1H chemical shift assignments for micasin
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