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. 1999 Aug 1;341(Pt 3):785–794.

Solution structure of a defensin-like peptide from platypus venom.

A M Torres 1, X Wang 1, J I Fletcher 1, D Alewood 1, P F Alewood 1, R Smith 1, R J Simpson 1, G M Nicholson 1, S K Sutherland 1, C H Gallagher 1, G F King 1, P W Kuchel 1
PMCID: PMC1220419  PMID: 10417345

Abstract

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 beta-sheet comprising residues 15-18 and 37-40 and a small 3(10) helix spanning residues 10-12. The overall three-dimensional fold is similar to that of beta-defensin-12, and similar to the sodium-channel neurotoxin ShI (Stichodactyla helianthus neurotoxin I). However, the side chains known to be functionally important in beta-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.

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Selected References

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