Non-coordinative metal selectivity bias in human metallothioneins metal-thiolate clusters.

ABSTRACT: Mammalian metallothioneins (MT-1 through MT-4) are a class of metal binding proteins containing two metal-thiolate clusters formed through the preferential coordination of d10 metals, Cu(i) and Zn(ii), by 20 conserved cysteine residues located in two protein domains. MT metalation (homometallic or heterometallic Zn(ii)/Cu(i) species) appears to be isoform specific and controlling zinc and copper concentrations to perform specific and distinct biological functions. Structural and functional relationships, and in vivo metalation studies, identified evolutionary features defining the metal-selectivity nature for MTs. Metallothionein-3 (MT-3) has been shown to possess the most pronounced Cu-thionein character forming Cu(i)-containing species more favorably than metallothionein-2 (MT-2), which

SUBMITTER: Calvo JS 

PROVIDER: S-EPMC6450656 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature