2hfr: Difference between revisions
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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 | <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 [ | <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=' | </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'>[ | <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 == | |||
[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 == | ||
| Line 14: | Line 17: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2hfr" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bommineni YR]] | ||
[[Category: | [[Category: Dai H]] | ||
[[Category: | [[Category: Gong Y]] | ||
[[Category: | [[Category: Prakash O]] | ||
[[Category: | [[Category: Zhang G]] | ||
Latest revision as of 19:37, 13 December 2023
solution structure of antimicrobial peptide Fowlicidin 3solution structure of antimicrobial peptide Fowlicidin 3
Structural highlights
FunctionCTHL3_CHICK May bind bacterial lipopolysaccharide (LPS). May have antimicrobial activity and play a role in the innate immune response (By similarity). Publication Abstract from PubMedCathelicidins 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 |
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