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| | ==solution structure of antimicrobial peptide Fowlicidin 3== | | ==solution structure of antimicrobial peptide Fowlicidin 3== |
| - | <StructureSection load='2hfr' size='340' side='right' caption='[[2hfr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2hfr' size='340' side='right'caption='[[2hfr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hfr]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HFR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HFR FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2amn|2amn]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hfr OCA], [http://pdbe.org/2hfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hfr RCSB], [http://www.ebi.ac.uk/pdbsum/2hfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hfr ProSAT]</span></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=2hfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hfr OCA], [https://pdbe.org/2hfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hfr RCSB], [https://www.ebi.ac.uk/pdbsum/2hfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hfr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CTHL3_CHICK CTHL3_CHICK]] May bind bacterial lipopolysaccharide (LPS). May have antimicrobial activity and play a role in the innate immune response (By similarity). | + | [https://www.uniprot.org/uniprot/CTHL3_CHICK CTHL3_CHICK] May bind bacterial lipopolysaccharide (LPS). May have antimicrobial activity and play a role in the innate immune response (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bommineni, Y R]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Dai, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Gong, Y]] | + | [[Category: Bommineni YR]] |
| - | [[Category: Prakash, O]] | + | [[Category: Dai H]] |
| - | [[Category: Zhang, G]] | + | [[Category: Gong Y]] |
| - | [[Category: Alpha helix]] | + | [[Category: Prakash O]] |
| - | [[Category: Antimicrobial protein]] | + | [[Category: Zhang G]] |
| Structural highlights
Function
CTHL3_CHICK May bind bacterial lipopolysaccharide (LPS). May have antimicrobial activity and play a role in the innate immune response (By similarity).
Publication Abstract from PubMed
Cathelicidins are an important family of cationic host defense peptides in vertebrates with both antimicrobial and immunomodulatory activities. Fowlicidin-1 and fowlicidin-2 are two newly identified chicken cathelicidins with potent antibacterial activities. Here we report structural and functional characterization of the putatively mature form of the third chicken cathelicidin, fowlicidin-3, for exploration of its therapeutic potential. NMR spectroscopy revealed that fowlicidin-3 comprises 27 amino-acid residues and adopts a predominantly alpha-helical structure extending from residue 9 to 25 with a slight kink induced by a glycine at position 17. It is highly potent against a broad range of Gram-negative and Gram-positive bacteria in vitro, including antibiotic-resistant strains, with minimum inhibitory concentrations in the range 1-2 microM. It kills bacteria quickly, permeabilizing cytoplasmic membranes immediately on coming into contact with them. Unlike many other host defense peptides with antimicrobial activities that are diminished by serum or salt, fowlicidin-3 retains bacteria-killing activities in the presence of 50% serum or physiological concentrations of salt. Furthermore, it is capable of suppressing lipopolysaccharide-induced expression of proinflammatory genes in mouse macrophage RAW264.7 cells, with nearly complete blockage at 10 microM. Fowlicidin-3 appears to be an excellent candidate for future development as a novel antimicrobial and antisepsis agent, particularly against antibiotic-resistant pathogens.
Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities.,Bommineni YR, Dai H, Gong YX, Soulages JL, Fernando SC, Desilva U, Prakash O, Zhang G FEBS J. 2007 Jan;274(2):418-28. PMID:17229147[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bommineni YR, Dai H, Gong YX, Soulages JL, Fernando SC, Desilva U, Prakash O, Zhang G. Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities. FEBS J. 2007 Jan;274(2):418-28. PMID:17229147 doi:EJB5589
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