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Issue 7, 2014
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Structural and computational insights into the versatility of cadmium binding to proteins

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Abstract

Cadmium is a highly toxic group XII metal, similar to zinc and mercury. Unlike zinc, which is one of the most common metal cofactors in biology, cadmium is highly toxic. Many Zn2+-binding proteins can bind Cd2+-ions without significantly affecting their structures. Here, the protein data bank is analysed with regard to protein–cadmium interactions, which shows that cadmium can bind to a variety of ion binding sites in proteins. Statistical analysis of Cd2+-side chain interactions is compared with a similar analysis of other ions. This analysis reveals that with regard to amino acid side-chain preference, Cd2+ is more similar to Mn2+ than to Zn2+ or Hg2+. Finally, the interaction energies of three native metal binding proteins are calculated where Cd2+ binds instead of Zn2+, Ca2+ or Cu2+. The interaction energies are decomposed into individual components whose contributions are discussed.

Graphical abstract: Structural and computational insights into the versatility of cadmium binding to proteins

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Publication details

The article was received on 08 Oct 2013, accepted on 02 Dec 2013 and first published on 03 Dec 2013


Article type: Paper
DOI: 10.1039/C3DT52810C
Citation: Dalton Trans., 2014,43, 2878-2887
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    Structural and computational insights into the versatility of cadmium binding to proteins

    R. Friedman, Dalton Trans., 2014, 43, 2878
    DOI: 10.1039/C3DT52810C

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