6FFK
Human apo-SOD1 bound to PtCl2(1R,2R-1,4-DACH
Summary for 6FFK
| Entry DOI | 10.2210/pdb6ffk/pdb |
| Related | 3re0 |
| Descriptor | Superoxide dismutase [Cu-Zn], PtCl2(1(R),2(R)-DACH) (3 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 64822.87 |
| Authors | Calderone, V.,Nativi, C.,Cantini, F.,Di Cesare Mannelli, L. (deposition date: 2018-01-08, release date: 2018-11-28, Last modification date: 2024-10-16) |
| Primary citation | Cantini, F.,Calderone, V.,Di Cesare Mannelli, L.,Korsak, M.,Gonnelli, L.,Francesconi, O.,Ghelardini, C.,Banci, L.,Nativi, C. Interaction of Half Oxa-/Halfcis-Platin Complex with Human Superoxide Dismutase and Induced Reduction of Neurotoxicity. ACS Med Chem Lett, 9:1094-1098, 2018 Cited by PubMed Abstract: The formation of amorphous protein aggregates containing human superoxide dismutase (hSOD1) is thought to be involved in amyotrophic lateral sclerosis onset. -Platin inhibits the oligomerization of apo hSOD1, but its toxicity precludes any possible use in therapy. Herein, we propose a less toxic platinum complex, namely oxa/-platin, as hSOD1 antiaggregation lead compound. Oxa/-platin is able to interact with hSOD1 in the disulfide oxidized apo form by binding cysteine 111 (Cys111). The mild neurotoxic phenomena induced in vitro and in vivo by oxa/-platin can be successfully reverted by using lypoyl derivatives, which do not interfere with the antiaggregation properties of the platin derivative. PubMed: 30429951DOI: 10.1021/acsmedchemlett.8b00199 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.94 Å) |
Structure validation
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