1B8W

DEFENSIN-LIKE PEPTIDE 1

Summary for 1B8W

• Entry DOI: 10.2210/pdb1b8w/pdb
• Descriptor: PROTEIN (DEFENSIN-LIKE PEPTIDE 1) (1 entity in total)
• Functional Keywords: toxin, platypus
• Biological source: Ornithorhynchus anatinus (platypus)
• Total number of polymer chains: 1
• Total formula weight: 4968.68

Authors

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. (deposition date: 1999-02-02, release date: 1999-09-15, Last modification date: 2024-10-16)

Primary citation

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.
Solution structure of a defensin-like peptide from platypus venom.
Biochem.J., 341:785-794, 1999

PubMed 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.

PubMed: 10417345
DOI: 10.1042/0264-6021:3410785

Experimental method

SOLUTION NMR