5ujg

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(New page: '''Unreleased structure''' The entry 5ujg is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (12:14, 6 November 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5ujg is ON HOLD
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==ovGRN12-35_3s==
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<StructureSection load='5ujg' size='340' side='right'caption='[[5ujg]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ujg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Opisthorchis_viverrini Opisthorchis viverrini]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UJG FirstGlance]. <br>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ujg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ujg OCA], [https://pdbe.org/5ujg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ujg RCSB], [https://www.ebi.ac.uk/pdbsum/5ujg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ujg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B8XSI4_9TREM B8XSI4_9TREM]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Granulins are a family of protein growth factors that are involved in cell proliferation. An orthologue of granulin from the human parasitic liver fluke Opisthorchis viverrini, known as Ov-GRN-1, induces angiogenesis and accelerates wound repair. Recombinant Ov-GRN-1 production is complex and poses an obstacle for clinical development. To identify the bioactive region(s) of Ov-GRN-1, four truncated N-terminal analogues were synthesized and characterized structurally using NMR spectroscopy. Peptides that contained only two native disulfide bonds lack the characteristic granulin beta-hairpin structure. Remarkably, the introduction of a non-native disulfide bond was critical for formation of beta-hairpin structure. Despite this structural difference, both two and three disulfide-bonded peptides drove proliferation of a human cholangiocyte cell line and demonstrated potent wound healing in mice. Peptides derived from Ov-GRN-1 are leads for novel wound healing therapeutics, as they are likely less immunogenic than the full-length protein and more convenient to produce.
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Authors:
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Development of a Potent Wound Healing Agent Based on the Liver Fluke Granulin Structural Fold.,Bansal PS, Smout MJ, Wilson D, Cobos Caceres C, Dastpeyman M, Sotillo J, Seifert J, Brindley PJ, Loukas A, Daly NL J Med Chem. 2017 May 25;60(10):4258-4266. doi: 10.1021/acs.jmedchem.7b00047. Epub, 2017 May 3. PMID:28425707<ref>PMID:28425707</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5ujg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Opisthorchis viverrini]]
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[[Category: Bansal P]]
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[[Category: Brindley P]]
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[[Category: Caceres CC]]
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[[Category: Daly N]]
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[[Category: Dastpeyman M]]
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[[Category: Loukas A]]
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[[Category: Seifert J]]
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[[Category: Smout M]]
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[[Category: Sotillo J]]
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[[Category: Wilson D]]

Current revision

ovGRN12-35_3s

PDB ID 5ujg

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