Abstract
Mammalian metallothioneins (MTs) are a class of low-molecular weight proteins containing 20 cysteine residues out of a total of 61 amino acid residues. MTs fold into two separate domains in the presence of certain metal ions [1,2]. Each domain binds metal ions in a polynuclear metalthiolate cluster with ligation through thiolates of the 20 cysteines residues [3]. Several NMR studies showed that the seven Cd(II) ions in the protein were positioned into the two clusters: α domain-with four Cd(II) ions and 11 cysteine residues, and β domain-with three Cd(II) ions and 9 cysteine residues [4–6]. The two spherical domains, with a similar diameter of 1.5–2.0 nm, are connected by a hinge region consisting of a conserved Lys-Lys-Ser (KKS) segment in the middle of the polypeptide chain [7].
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Xiong, Y., Zhou, Y., Chen, Y., Ru, B. (1999). Molecular splicing of metallothionein — study on domains of metallothionein. In: Klaassen, C.D. (eds) Metallothionein IV. Advances in Life Sciences. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8847-9_19
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DOI: https://doi.org/10.1007/978-3-0348-8847-9_19
Publisher Name: Birkhäuser, Basel
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