1b8w | pdb_00001b8w

DEFENSIN-LIKE PEPTIDE 1

spinqualitylabelsall models 1b8w Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1b8w is a 1 chain structure with sequence from Ornithorhynchus anatinus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DLP1_ORNAN Does not show antimicrobial, myotoxic, hemolytic and cell-promoting activities. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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