4Z46
X-ray structure of the bis-platinum lysozyme adduct formed in the reaction between the protein and the two drugs Cisplatin and Oxaliplatin
Summary for 4Z46
| Entry DOI | 10.2210/pdb4z46/pdb |
| Descriptor | Lysozyme C, 1,2-ETHANEDIOL, NITRATE ION, ... (7 entities in total) |
| Functional Keywords | cisplatin, oxaliplatin, protein platination, anticancer drugs, hydrolase |
| Biological source | Gallus gallus (Chicken) |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 1 |
| Total formula weight | 15668.63 |
| Authors | Merlino, A. (deposition date: 2015-04-01, release date: 2015-05-27, Last modification date: 2024-10-16) |
| Primary citation | Marasco, D.,Messori, L.,Marzo, T.,Merlino, A. Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme. Dalton Trans, 44:10392-10398, 2015 Cited by PubMed Abstract: The model protein hen egg white lysozyme was challenged with oxaliplatin and cisplatin. ESI mass spectrometry, surface plasmon resonance and thermal shift analyses demonstrate the formation of a bis-platinum adduct, though in very small amounts. Crystals of the bis-platinum adduct were obtained using two different preparations and the X-ray structures were solved at 1.85 Å and 1.95 Å resolution. Overall, the obtained data point out that, under the analyzed conditions, the two Pt drugs have similar affinities for the protein, but bind on its surface at two non-overlapping sites. In other words, these two drugs manifest a significantly different reactivity with this model protein and do not compete for the same protein binding sites. PubMed: 25974859DOI: 10.1039/c5dt01279a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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