2hfr

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{{Seed}}
 
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[[Image:2hfr.png|left|200px]]
 
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==solution structure of antimicrobial peptide Fowlicidin 3==
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The line below this paragraph, containing "STRUCTURE_2hfr", creates the "Structure Box" on the page.
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<StructureSection load='2hfr' size='340' side='right'caption='[[2hfr]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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{{STRUCTURE_2hfr| PDB=2hfr | SCENE= }}
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</table>
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== Function ==
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===solution structure of antimicrobial peptide Fowlicidin 3===
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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<ref>PMID:17229147</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17229147}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2hfr" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17229147 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17229147}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Gallus gallus]]
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2HFR is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HFR OCA].
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[[Category: Large Structures]]
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[[Category: Bommineni YR]]
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==Reference==
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[[Category: Dai H]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17229147 17229147]
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[[Category: Gong Y]]
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[[Category: Single protein]]
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[[Category: Prakash O]]
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[[Category: Bommineni, Y R.]]
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[[Category: Zhang G]]
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[[Category: Dai, H.]]
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[[Category: Gong, Y.]]
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[[Category: Prakash, O.]]
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[[Category: Zhang, G.]]
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[[Category: Alpha helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:51:47 2008''
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Current revision

solution structure of antimicrobial peptide Fowlicidin 3

PDB ID 2hfr

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