Solution structure of a defensin-like peptide from platypus venom

Autor: Torres, A M, Wang, X, Fletcher, J I, Alewood, D, Alewood, P F, Smith, R, Simpson, R J, Nicholson, G M, Sutherland, S K, Gallagher, C H, King, G F, Kuchel, P W
Jazyk: angličtina
Rok vydání: 1999
Předmět:
Popis: 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.
Databáze: OpenAIRE