Solution structure of a defensin-like peptide from platypus venom

Three defensin-like peptides (DLPs) were isolated from platypus venom and sequenced. One of these peptides, DLP-1, was synthesized chemically and its three-dimensional structure was determined using NMR spectroscopy. The main structural elements of this 42-residue peptide were an anti-parallel β-she...

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Bibliographic Details
Published in:Biochemical journal 1999-08, Vol.341 (3), p.785-794
Main Authors: TORRES, Allan M., WANG, Xiuhong, FLETCHER, Jamie I., ALEWOOD, Dianne, ALEWOOD, Paul F., SMITH, Ross, SIMPSON, Richard J., NICHOLSON, Graham M., SUTHERLAND, Struan K., GALLAGHER, Cliff H., KING, Glenn F., KUCHEL, Philip W.
Format: Article
Language:English
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Summary:Three defensin-like peptides (DLPs) were isolated from platypus venom and sequenced. One of these peptides, DLP-1, was synthesized chemically and its three-dimensional structure was determined using NMR spectroscopy. The main structural elements of this 42-residue peptide were an anti-parallel β-sheet comprising residues 15-18 and 37-40 and a small 310 helix spanning residues 10-12. The overall three-dimensional fold is similar to that of β-defensin-12, and similar to the sodium-channel neurotoxin ShI (Stichodactyla helianthusneurotoxin I). However, the side chains known to be functionally important in β-defensin-12 and ShI are not conserved in DLP-1, suggesting that it has a different biological function. Consistent with this contention, we showed that DLP-1 possesses no anti-microbial properties and has no observable activity on rat dorsal-root-ganglion sodium-channel currents.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3410785