1zue: Difference between revisions
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==Revised Solution Structure of DLP-2== | |||
<StructureSection load='1zue' size='340' side='right'caption='[[1zue]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zue]] 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=1ZUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MED:D-METHIONINE'>MED</scene></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=1zue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zue OCA], [https://pdbe.org/1zue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zue RCSB], [https://www.ebi.ac.uk/pdbsum/1zue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zue 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 1zue" 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]] | |||
Latest revision as of 07:46, 30 October 2024
Revised Solution Structure of DLP-2
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