Solution structure of a defensin-like peptide from platypus venom
Journal Title
BIOCHEMICAL JOURNAL
Publication Type
Journal Article
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.
Publisher
PORTLAND PRESS
Keywords
NUCLEAR-MAGNETIC-RESONANCE; BRAIN NATRIURETIC PEPTIDE; CROTALUS-VIRIDIS-VIRIDIS; COUPLING-CONSTANTS; ORNITHORHYNCHUS-ANATINUS; DISTANCE GEOMETRY; NMR-SPECTROSCOPY; MYOTOXIN-A; PROTEINS; SEQUENCE
Rights Notice
Refer to copyright notice on published article.


Creation Date: 1999-08-01 12:00:00
Last Modified: 0001-01-01 12:00:00
An error has occurred. This application may no longer respond until reloaded. Reload 🗙