Structural highlights
Function
DEFBL_ORNAN Has antimicrobial activity.
Publication Abstract from PubMed
The three-dimensional structure of a chemically synthesized peptide that we have called 'intermediate' defensin-like peptide (Int-DLP), from the platypus genome, was determined by nuclear magnetic resonance (NMR) spectroscopy; and its antimicrobial activity was investigated. The overall structural fold of Int-DLP was similar to that of the DLPs and beta-defensins, however the presence of a third antiparallel beta-strand makes its structure more similar to the beta-defensins than the DLPs. Int-DLP displayed potent antimicrobial activity against Staphylococcus aureus and Pseudomonas aeruginosa. The four arginine residues at the N-terminus of Int-DLP did not affect the overall fold, but were important for its antimicrobial potency.
Structure and antimicrobial activity of platypus 'intermediate' defensin-like peptide.,Torres AM, Bansal P, Koh JM, Pages G, Wu MJ, Kuchel PW FEBS Lett. 2014 May 2;588(9):1821-6. doi: 10.1016/j.febslet.2014.03.044. Epub, 2014 Mar 30. PMID:24694388[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Torres AM, Bansal P, Koh JM, Pages G, Wu MJ, Kuchel PW. Structure and antimicrobial activity of platypus 'intermediate' defensin-like peptide. FEBS Lett. 2014 May 2;588(9):1821-6. doi: 10.1016/j.febslet.2014.03.044. Epub, 2014 Mar 30. PMID:24694388 doi:http://dx.doi.org/10.1016/j.febslet.2014.03.044
