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Solution structure of a defensin-like peptide from platypus venom


Torres, AM; Wang, XH; Fletcher, JI; Alewood, D; Alewood, PF; Smith, R; Simpson, RJ; Nicholson, GM; Sutherland, SK; Gallagher, CH; King, GF; Kuchel, PW
1999-08-01
BIOCHEMICAL JOURNAL
Journal Article
341
785-794
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.
PORTLAND PRESS
NUCLEAR-MAGNETIC-RESONANCE; BRAIN NATRIURETIC PEPTIDE; CROTALUS-VIRIDIS-VIRIDIS; COUPLING-CONSTANTS; ORNITHORHYNCHUS-ANATINUS; DISTANCE GEOMETRY; NMR-SPECTROSCOPY; MYOTOXIN-A; PROTEINS; SEQUENCE
10.1042/0264-6021:3410785
Refer to copyright notice on published article.