3RE0

Crystal structure of human apo Cu,Zn superoxide dismutase (SOD1) complexed with cisplatin

Summary for 3RE0

• Entry DOI: 10.2210/pdb3re0/pdb
• Related: 3ECU 3ECV 3ECW
• Descriptor: Superoxide dismutase [Cu-Zn], Cisplatin (3 entities in total)
• Functional Keywords: sod1, cisplatin, als, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P00441
• Total number of polymer chains: 4
• Total formula weight: 64210.38

Authors

Bertini, I.,Blazevits, O.,Calderone, V.,Jaifei, M.,Vieru, M.,Amori, I.,Cozzolino, M.,Carri, M.T.,Banci, L. (deposition date: 2011-04-02, release date: 2012-04-25, Last modification date: 2024-10-30)

Primary citation

Banci, L.,Bertini, I.,Blazevits, O.,Calderone, V.,Cantini, F.,Mao, J.,Trapananti, A.,Vieru, M.,Amori, I.,Cozzolino, M.,Carri, M.T.
Interaction of cisplatin with human superoxide dismutase.
J.Am.Chem.Soc., 134:7009-7014, 2012

PubMed Abstract: cis-Diamminedichloroplatinum(II) (cisplatin) is able to interact with human superoxide dismutase (hSOD1) in the disulfide oxidized apo form with a dissociation constant of 37 ± 3 μM through binding cysteine 111 (Cys111) located at the edge of the subunit interface. It also binds to Cu(2)-Zn(2) and Zn(2)-Zn(2) forms of hSOD1. Cisplatin inhibits aggregation of demetalated oxidized hSOD1, and it is further able to dissolve and monomerize oxidized hSOD1 oligomers in vitro and in cell, thus indicating its potential as a leading compound for amyotrophic lateral sclerosis.

PubMed: 22471402
DOI: 10.1021/ja211591n

Experimental method

X-RAY DIFFRACTION (2.28 Å)