7NPM
X-ray structure of the adduct formed upon reaction of oxaliplatin with human angiogenin
This is a non-PDB format compatible entry.
Summary for 7NPM
| Entry DOI | 10.2210/pdb7npm/pdb |
| Descriptor | Angiogenin, PLATINUM (II) ION, D(-)-TARTARIC ACID, ... (4 entities in total) |
| Functional Keywords | oxaliplatin, cancer, angiogenesis, protein metallation, angiogenin, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 14679.11 |
| Authors | Ferraro, G.,Merlino, A. (deposition date: 2021-02-27, release date: 2022-03-23, Last modification date: 2024-11-13) |
| Primary citation | Marzo, T.,Ferraro, G.,Cucci, L.M.,Pratesi, A.,Hansson, O.,Satriano, C.,Merlino, A.,La Mendola, D. Oxaliplatin inhibits angiogenin proliferative and cell migration effects in prostate cancer cells. J.Inorg.Biochem., 226:111657-111657, 2022 Cited by PubMed Abstract: Angiogenin (Ang) is a potent angiogenic protein that is overexpressed in many types of cancer at concentration values correlated to the tumor aggressiveness. Here, by means of an integrated multi-technique approach based on crystallographic, spectrometric and spectroscopic analyses, we demonstrate that the anti-cancer drug oxaliplatin efficiently binds angiogenin. Microscopy cellular studies, carried out on the prostate cancer cell (PC-3) line , show that oxaliplatin inhibits the angiogenin prompting effect on cell proliferation and migration, which are typical features of angiogenesis process. Overall, our findings point to angiogenin as a possible target of oxaliplatin, thus suggesting a potential novel mechanism for the antineoplastic activity of this platinum drug and opening the avenue to novel approaches in the combined anti-cancer anti-angiogenic therapy. PubMed: 34784565DOI: 10.1016/j.jinorgbio.2021.111657 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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