Challenging conventional wisdom: single domain metallothioneins

  • Duncan E. K. Sutherland, Martin J. Stillman
  • Metallomics, January 2014, Oxford University Press (OUP)
  • DOI: 10.1039/c3mt00216k

Single Domain Metallothioneins

What is it about?

Metal ions, such as copper and zinc, are necessary for human health. Metallothionein (MT), a protein, is considered key in the healthy balance of these metals. The traditional view of MT is that metals are bound into two domains. However, until recently the exact way in which it divided these metals was largely unknown. This review describes a new single domain model of metal binding and explains its importance in terms of protein-protein interactions and the balance of metals in humans.

Why is it important?

This review focuses on the recent mechanistic studies of metallothionein (MT). Importantly, it provides evidence that the traditional two-domain view of MT is in fact the exception, and that in cases of metal ion deficiency, or metal ion excess, the protein adopts a single domain structure. This new view of MT is critical in our understanding of metal ion homeostasis, possible protein-protein interactions, as well as any potential future therapeutic uses of the protein.

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The following have contributed to this page: Martin Stillman