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1zuf
From Proteopedia
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| - | [[Image:1zuf.gif|left|200px]] | ||
| - | + | ==Solution Structure of DLP-4== | |
| - | + | <StructureSection load='1zuf' size='340' side='right'caption='[[1zuf]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1zuf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ornithorhynchus_anatinus Ornithorhynchus anatinus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUF FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zuf OCA], [https://pdbe.org/1zuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zuf RCSB], [https://www.ebi.ac.uk/pdbsum/1zuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zuf ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | ''' | + | [https://www.uniprot.org/uniprot/DLP2_ORNAN DLP2_ORNAN] Does not show antimicrobial, myotoxic, hemolytic and cell-promoting activities.<ref>PMID:10417345</ref> |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| - | == | + | |
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. | 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. | ||
| - | + | 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<ref>PMID:16033333</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1zuf" style="background-color:#fffaf0;"></div> |
| - | [[Category: Alewood | + | == References == |
| - | [[Category: Bansal | + | <references/> |
| - | [[Category: Geraghty | + | __TOC__ |
| - | [[Category: Kuchel | + | </StructureSection> |
| - | [[Category: Torres | + | [[Category: Large Structures]] |
| - | [[Category: Tsampazi | + | [[Category: Ornithorhynchus anatinus]] |
| - | + | [[Category: Alewood PF]] | |
| - | + | [[Category: Bansal PS]] | |
| - | + | [[Category: Geraghty DP]] | |
| + | [[Category: Kuchel PW]] | ||
| + | [[Category: Torres AM]] | ||
| + | [[Category: Tsampazi C]] | ||
Current revision
Solution Structure of DLP-4
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