5UJH
ov-GRN12-34
Summary for 5UJH
| Entry DOI | 10.2210/pdb5ujh/pdb |
| Related | 5UJG |
| NMR Information | BMRB: 30233 |
| Descriptor | Granulin (1 entity in total) |
| Functional Keywords | wound healing agent, structure calculation, structure from cyana 3.97, cytokine |
| Biological source | Opisthorchis viverrini |
| Total number of polymer chains | 1 |
| Total formula weight | 2457.81 |
| Authors | Bansal, P.,Smout, M.,Wilson, D.,Caceres, C.C.,Dastpeyman, M.,Sotillo, J.,Seifert, J.,Brindley, P.,Loukas, A.,Daly, N. (deposition date: 2017-01-18, release date: 2018-01-24, Last modification date: 2024-10-23) |
| Primary citation | Bansal, P.S.,Smout, M.J.,Wilson, D.,Cobos Caceres, C.,Dastpeyman, M.,Sotillo, J.,Seifert, J.,Brindley, P.J.,Loukas, A.,Daly, N.L. Development of a Potent Wound Healing Agent Based on the Liver Fluke Granulin Structural Fold. J. Med. Chem., 60:4258-4266, 2017 Cited by PubMed Abstract: 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 β-hairpin structure. Remarkably, the introduction of a non-native disulfide bond was critical for formation of β-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. PubMed: 28425707DOI: 10.1021/acs.jmedchem.7b00047 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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