4RTE
The X-ray structure of bovine pancreatic ribonuclease incubated in the presence of an excess of cisplatin (1:10 ratio)
Summary for 4RTE
| Entry DOI | 10.2210/pdb4rte/pdb |
| Related | 4OT4 |
| Descriptor | Ribonuclease pancreatic, Cisplatin, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | rnase fold, rna cleavage, hydrolase |
| Biological source | Bos taurus (bovine,cow,domestic cattle,domestic cow) |
| Cellular location | Secreted: P61823 |
| Total number of polymer chains | 1 |
| Total formula weight | 15014.86 |
| Authors | Russo Krauss, I.,Merlino, A. (deposition date: 2014-11-14, release date: 2015-03-25, Last modification date: 2024-11-06) |
| Primary citation | Picone, D.,Donnarumma, F.,Ferraro, G.,Russo Krauss, I.,Fagagnini, A.,Gotte, G.,Merlino, A. Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability. J.Inorg.Biochem., 146:37-43, 2015 Cited by PubMed Abstract: The reaction between cis-diamminedichloroplatinum(II) (CDDP), cisplatin, a common anticancer drug, and bovine pancreatic ribonuclease (RNase A), induces extensive protein aggregation, leading to the formation of one dimer, one trimer and higher oligomers whose yields depend on cisplatin/protein ratio. Structural and functional properties of the purified platinated species, together with their spontaneous dissociation and thermally induced denaturation, have been characterized. Platinated species preserve a significant, although reduced, ribonuclease activity. The high resistance of the dimers against dissociation and the different thermal unfolding profiles suggest a quaternary structure different from those of the well-known swapped dimers of RNase A. PubMed: 25756333DOI: 10.1016/j.jinorgbio.2015.02.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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