1d6b: Difference between revisions
New page: left|200px<br /><applet load="1d6b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d6b" /> '''SOLUTION STRUCTURE OF DEFENSIN-LIKE PEPTIDE-... |
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== | ==SOLUTION STRUCTURE OF DEFENSIN-LIKE PEPTIDE-2 (DLP-2) FROM PLATYPUS VENOM== | ||
The venom of the male Australian duck-billed platypus contains a family of | <StructureSection load='1d6b' size='340' side='right'caption='[[1d6b]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1d6b]] 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=1D6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D6B 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6b OCA], [https://pdbe.org/1d6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d6b RCSB], [https://www.ebi.ac.uk/pdbsum/1d6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d6b 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 venom of the male Australian duck-billed platypus contains a family of four polypeptides of appox. 5 kDa, which are referred to as defensin-like peptides (DLPs). They are unique in that their amino acid sequences have no significant similarities to those of any known peptides; however, the tertiary structure of one of them, DLP-1, has recently been shown to be similar to beta-defensin-12 and to the sodium neurotoxin peptide ShI (Stichodactyla helianthus neurotoxin I). Although DLPs are the major peptides in the platypus venom, little is known about their biological roles. In this study, we determined the three-dimensional structure of DLP-2 by NMR spectroscopy, with the aim of gaining insights into the natural function of the DLPs in platypus venom. The DLP-2 structure was found to incorporate a short helix that spans residues 9-12, and an antiparallel beta-sheet defined by residues 15-18 and 37-40. The overall fold and cysteine-pairing pattern of DLP-2 were found to be similar to those of DLP-1, and hence beta-defensin-12; however, the sequence similarities between the three molecules are relatively small. The distinct structural fold of the DLP-1, DLP-2, and beta-defensin-12 is based upon several key residues that include six cysteines. DLP-3 and DLP-4 are also likely to be folded similarly since they have high sequence similarity with DLP-2. The DLPs, and beta-defensin-12 may thus be grouped together into a class of polypeptide molecules which have a common or very similar global fold. The fact that the DLPs did not display antimicrobial, myotoxic, or cell-growth-promoting activities implies that the nature of the side chains in this group of peptides is likely to play an important role in defining the biological function(s). | |||
Defensin-like peptide-2 from platypus venom: member of a class of peptides with a distinct structural fold.,Torres AM, de Plater GM, Doverskog M, Birinyi-Strachan LC, Nicholson GM, Gallagher CH, Kuchel PW Biochem J. 2000 Jun 15;348 Pt 3:649-56. PMID:10839998<ref>PMID:10839998</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1d6b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ornithorhynchus anatinus]] | [[Category: Ornithorhynchus anatinus]] | ||
[[Category: | [[Category: C Birinyi-Strachan L]] | ||
[[Category: | [[Category: De Plater GM]] | ||
[[Category: Doverskog | [[Category: Doverskog M]] | ||
[[Category: Gallagher | [[Category: Gallagher CH]] | ||
[[Category: Kuchel | [[Category: Kuchel PW]] | ||
[[Category: Nicholson | [[Category: Nicholson GM]] | ||
[[Category: Torres AM]] | |||
[[Category: Torres | |||
Latest revision as of 09:31, 30 October 2024
SOLUTION STRUCTURE OF DEFENSIN-LIKE PEPTIDE-2 (DLP-2) FROM PLATYPUS VENOMSOLUTION STRUCTURE OF DEFENSIN-LIKE PEPTIDE-2 (DLP-2) FROM PLATYPUS VENOM
Structural highlights
FunctionDLP2_ORNAN Does not show antimicrobial, myotoxic, hemolytic and cell-promoting activities.[1] Publication Abstract from PubMedThe venom of the male Australian duck-billed platypus contains a family of four polypeptides of appox. 5 kDa, which are referred to as defensin-like peptides (DLPs). They are unique in that their amino acid sequences have no significant similarities to those of any known peptides; however, the tertiary structure of one of them, DLP-1, has recently been shown to be similar to beta-defensin-12 and to the sodium neurotoxin peptide ShI (Stichodactyla helianthus neurotoxin I). Although DLPs are the major peptides in the platypus venom, little is known about their biological roles. In this study, we determined the three-dimensional structure of DLP-2 by NMR spectroscopy, with the aim of gaining insights into the natural function of the DLPs in platypus venom. The DLP-2 structure was found to incorporate a short helix that spans residues 9-12, and an antiparallel beta-sheet defined by residues 15-18 and 37-40. The overall fold and cysteine-pairing pattern of DLP-2 were found to be similar to those of DLP-1, and hence beta-defensin-12; however, the sequence similarities between the three molecules are relatively small. The distinct structural fold of the DLP-1, DLP-2, and beta-defensin-12 is based upon several key residues that include six cysteines. DLP-3 and DLP-4 are also likely to be folded similarly since they have high sequence similarity with DLP-2. The DLPs, and beta-defensin-12 may thus be grouped together into a class of polypeptide molecules which have a common or very similar global fold. The fact that the DLPs did not display antimicrobial, myotoxic, or cell-growth-promoting activities implies that the nature of the side chains in this group of peptides is likely to play an important role in defining the biological function(s). Defensin-like peptide-2 from platypus venom: member of a class of peptides with a distinct structural fold.,Torres AM, de Plater GM, Doverskog M, Birinyi-Strachan LC, Nicholson GM, Gallagher CH, Kuchel PW Biochem J. 2000 Jun 15;348 Pt 3:649-56. PMID:10839998[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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