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| - | [[Image:2hfr.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2hfr| PDB=2hfr | SCENE= }} | | {{STRUCTURE_2hfr| PDB=2hfr | SCENE= }} |
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| - | '''solution structure of antimicrobial peptide Fowlicidin 3'''
| + | ===solution structure of antimicrobial peptide Fowlicidin 3=== |
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| - | ==Overview==
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17229147}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17229147 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17229147}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2HFR is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HFR OCA]. | + | 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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| | ==Reference== | | ==Reference== |
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| | [[Category: Zhang, G.]] | | [[Category: Zhang, G.]] |
| | [[Category: Alpha helix]] | | [[Category: Alpha helix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:14:22 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:51:47 2008'' |
Revision as of 04:51, 29 July 2008
Template:STRUCTURE 2hfr
solution structure of antimicrobial peptide Fowlicidin 3
Template:ABSTRACT PUBMED 17229147
About this Structure
2HFR is a Single protein structure. Full experimental information is available from OCA.
Reference
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
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