1ZUF
Solution Structure of DLP-4
Summary for 1ZUF
Entry DOI | 10.2210/pdb1zuf/pdb |
Related | 1D6B 1ZUE |
Descriptor | Defensin-like peptide 2/4 (1 entity in total) |
Functional Keywords | helix, antiparallel beta-sheet, toxin |
Cellular location | Secreted: P82140 |
Total number of polymer chains | 1 |
Total formula weight | 5121.90 |
Authors | Torres, A.M.,Tsampazi, C.,Geraghty, D.P.,Bansal, P.S.,Alewood, P.F.,Kuchel, P.W. (deposition date: 2005-05-31, release date: 2005-08-02, Last modification date: 2022-03-02) |
Primary citation | Torres, A.M.,Tsampazi, C.,Geraghty, D.P.,Bansal, P.S.,Alewood, P.F.,Kuchel, P.W. D-amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties. Biochem.J., 391:215-220, 2005 Cited by PubMed Abstract: The 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. PubMed: 16033333DOI: 10.1042/BJ20050900 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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