Abstract
The class of proteins known as metallothionein is presently only defined structurally since the physiological function is unresolved. These proteins are characterized by being low molecular weight (<10,000 daltons) polypeptides enriched in cysteinyl residues and containing numerous metal ions coordinated within polynuclear metal-thiolate clusters. The structure of mammalian Cd, Zn-metallothionein has been resolved by both x-ray analysis and NMR spectroscopy (1,2). The molecule exists as a two domain protein with the seven metal ions coordinated tetrahedrally in two polynuclear clusters with the 20 cysteines serving as terminal and bridging ligands.
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© 1988 Plenum Press, New York
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Winge, D.R. (1988). The Cu-Thiolate Cluster in Mutants of Yeast Metallothionein. In: Hurley, L.S., Keen, C.L., Lönnerdal, B., Rucker, R.B. (eds) Trace Elements in Man and Animals 6. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0723-5_12
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DOI: https://doi.org/10.1007/978-1-4613-0723-5_12
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