MT2A binds zinc

Stable Identifier
R-HSA-5662598
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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The metallothionein MT2A binds 7 atoms of zinc(II) in two clusters, one at the N-terminal beta domain and one at the C-terminal alpha domain (Stillman et al. 2000, Yang et al. 2007). The cluster at the alpha domain is more stable than the cluster at the beta domain, making the beta domain a better zinc donor (Jiang et al. 2000). Each cluster assembles independently (Jiang et al. 2000).

Literature References
PubMed ID Title Journal Year
17224279 High-yield expression in Escherichia coli of soluble human MT2A with native functions

Yang, F, Zhou, M, He, Z, Liu, X, Sun, L, Sun, Y, Chen, Z

Protein Expr. Purif. 2007
10830841 Circular dichroism, kinetic and mass spectrometric studies of copper(I) and mercury(II) binding to metallothionein

Stillman, MJ, Thomas, D, Trevithick, C, Guo, X, Siu, M

J. Inorg. Biochem. 2000
10716985 Zinc transfer potentials of the alpha - and beta-clusters of metallothionein are affected by domain interactions in the whole molecule

Jiang, LJ, Vasák, M, Vallee, BL, Maret, W

Proc. Natl. Acad. Sci. U.S.A. 2000
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