2HFR
solution structure of antimicrobial peptide Fowlicidin 3
Summary for 2HFR
| Entry DOI | 10.2210/pdb2hfr/pdb |
| Related | 2amn |
| Descriptor | Fowlicidin-3 (1 entity in total) |
| Functional Keywords | alpha helix, antimicrobial protein |
| Cellular location | Secreted (By similarity): Q2IAL6 |
| Total number of polymer chains | 1 |
| Total formula weight | 3101.78 |
| Authors | Bommineni, Y.R.,Dai, H.,Gong, Y.,Prakash, O.,Zhang, G. (deposition date: 2006-06-26, release date: 2007-04-17, Last modification date: 2024-05-29) |
| Primary citation | Bommineni, Y.R.,Dai, H.,Gong, Y.X.,Soulages, J.L.,Fernando, S.C.,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., 274:418-428, 2007 Cited by PubMed Abstract: 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. PubMed: 17229147DOI: 10.1111/j.1742-4658.2006.05589.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
