| Literature DB >> 10417345 |
A M Torres1, X Wang, J I Fletcher, D Alewood, P F Alewood, R Smith, R J Simpson, G M Nicholson, S K Sutherland, C H Gallagher, G F King, P W Kuchel.
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.Entities:
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Year: 1999 PMID： 10417345 PMCID： PMC1220419
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857