1b8w | pdb_00001b8w
DEFENSIN-LIKE PEPTIDE 1
Overview
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.
About this Structure
1B8W is a Single protein structure of sequence from Ornithorhynchus anatinus. Full crystallographic information is available from OCA.
Reference
Solution structure of a defensin-like peptide from platypus venom., Torres AM, Wang X, Fletcher JI, Alewood D, Alewood PF, Smith R, Simpson RJ, Nicholson GM, Sutherland SK, Gallagher CH, King GF, Kuchel PW, Biochem J. 1999 Aug 1;341 ( Pt 3):785-94. PMID:10417345 Page seeded by OCA on Fri May 2 11:13:10 2008
