5MIK
X-ray structure of carboplatin-encapsulated horse spleen apoferritin (rotating anode data)
Summary for 5MIK
Entry DOI | 10.2210/pdb5mik/pdb |
Descriptor | Ferritin light chain, CADMIUM ION, CHLORIDE ION, ... (7 entities in total) |
Functional Keywords | metal transport |
Biological source | Equus caballus (Horse) |
Total number of polymer chains | 1 |
Total formula weight | 21885.71 |
Authors | Pontillo, N.,Ferraro, G.,Helliwell, J.R.,Merlino, A. (deposition date: 2016-11-28, release date: 2017-03-15, Last modification date: 2024-01-17) |
Primary citation | Pontillo, N.,Ferraro, G.,Helliwell, J.R.,Amoresano, A.,Merlino, A. X-ray Structure of the Carboplatin-Loaded Apo-Ferritin Nanocage. ACS Med Chem Lett, 8:433-437, 2017 Cited by PubMed Abstract: The second-generation Pt anticancer agent carboplatin (CBDCA) was encapsulated within the apo horse spleen ferritin (AFt) nanocage, and the X-ray structure of the drug-loaded protein was refined at 1.49 Å resolution. Two Pt binding sites, different from the one observed in the cisplatin-encapsulated AFt, were identified in Ft subunits by inspection of anomalous electron density maps at two wavelengths and difference Fourier electron density maps, which provide the necessary sensitivity to discriminate between Pt from CBDCA and Cd ions that are present in the crystallization conditions. Pt centers coordinate to the NE2 atom of His49 and to the NE2 atom of His132, both on the inner surface of the Ft nanocage. PubMed: 28435532DOI: 10.1021/acsmedchemlett.7b00025 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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