2hfr: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:2hfr.gif|left|200px]]
{{Seed}}
[[Image:2hfr.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hfr|  PDB=2hfr  |  SCENE=  }}  
{{STRUCTURE_2hfr|  PDB=2hfr  |  SCENE=  }}  


'''solution structure of antimicrobial peptide Fowlicidin 3'''
===solution structure of antimicrobial peptide Fowlicidin 3===




==Overview==
<!--  
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.
-->
{{ABSTRACT_PUBMED_17229147}}


==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].  


==Reference==
==Reference==
Line 27: Line 31:
[[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

File:2hfr.png

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

Page seeded by OCA on Tue Jul 29 07:51:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2hfr&oldid=733516"