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Zinc-Binding Sites in Proteins

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Encyclopedia of Metalloproteins

Definitions

The inner shell coordination properties of zinc enzymes have led to the identification of four types of zinc-binding sites: Catalytic, Cocatalytic, Structural, and Protein Interface. Zinc has also been found to form clusters in a number of proteins involved in DNA/RNA binding and in distribution of zinc to other proteins.

Background

Zinc, copper, and iron are the three most prevalent metals in biological systems. The proof of the nutritional importance of zinc spanned nearly 100 years from the first studies in the fungus Aspergillus niger by Raulin in 1869 to that in humans by Prasad in1963 (Zinc Deficiency). The rapid changes in technology over the last several decades have led to establishing its importance on the molecular level. Protein-bound zinc is involved in a wide variety of metabolic processes including carbohydrate, lipid, nucleic acid and protein synthesis, and degradation (Auld 2005). Zinc is the only metal to have representatives in all six of the...

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References

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Correspondence to David S. Auld .

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Auld, D.S. (2013). Zinc-Binding Sites in Proteins. In: Kretsinger, R.H., Uversky, V.N., Permyakov, E.A. (eds) Encyclopedia of Metalloproteins. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1533-6_182

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