1zue
Revised Solution Structure of DLP-2Revised Solution Structure of DLP-2
Structural highlights
FunctionDLP2_ORNAN Does not show antimicrobial, myotoxic, hemolytic and cell-promoting activities.[1] Publication Abstract from PubMedThe recent discovery that the natriuretic peptide OvCNPb (Ornithorhynchus venom C-type natriuretic peptide B) from platypus (Ornithorynchus anatinus) venom contains a D-amino acid residue suggested that other D-amino-acid-containing peptides might be present in the venom. In the present study, we show that DLP-2 (defensin-like peptide-2), a 42-amino-acid residue polypeptide in the platypus venom, also contains a D-amino acid residue, D-methionine, at position 2, while DLP-4, which has an identical amino acid sequence, has all amino acids in the L-form. These findings were supported further by the detection of isomerase activity in the platypus gland venom extract that converts DLP-4 into DLP-2. In the light of this new information, the tertiary structure of DLP-2 was recalculated using a new structural template with D-Met2. The structure of DLP-4 was also determined in order to evaluate the effect of a D-amino acid at position 2 on the structure and possibly to explain the large retention time difference observed for the two molecules in reverse-phase HPLC. The solution structures of the DLP-2 and DLP-4 are very similar to each other and to the earlier reported structure of DLP-2, which assumed that all amino acids were in the L-form. Our results suggest that the incorporation of the D-amino acid at position 2 has minimal effect on the overall fold in solution. D-amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties.,Torres AM, Tsampazi C, Geraghty DP, Bansal PS, Alewood PF, Kuchel PW Biochem J. 2005 Oct 15;391(Pt 2):215-20. PMID:16033333[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||