MT1A binds cadmium

Stable Identifier
Reaction [binding]
Homo sapiens
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MT1A binds 7 atoms of cadmium(II), 3 atoms at the N-terminal beta domain and 4 atoms at the C-terminal alpha domain (Rigby Duncan et al. 2008, Sunderland and Stillman 2008, Sutherland et al. 2012). A fifth cadmium atom bound to the alpha domain may be an intermediate formed during metal exchange (Rigby Duncan et al. 2008). Binding of cadmium is non-cooperative (Rigby Duncan and Stillman 2007, Sunderland and Stillman 2008). As inferred from mouse Mt1, MT1A may show less preference for zinc compared with cadmium and may therefore serve more than other metallothionein isoforms to detoxify cadmium.

Literature References
PubMed ID Title Journal Year
18429853 Metal exchange in metallothioneins: a novel structurally significant Cd(5) species in the alpha domain of human metallothionein 1a

Rigby Duncan, KE, Kirby, CW, Stillman, MJ

FEBS J. 2008
18533113 Noncooperative cadmium(II) binding to human metallothionein 1a

Sutherland, DE, Stillman, MJ

Biochem. Biophys. Res. Commun. 2008
22982309 Modeling the Zn(2+) and Cd(2+) metalation mechanism in mammalian metallothionein 1a

Sutherland, DE, Summers, KL, Stillman, MJ

Biochem. Biophys. Res. Commun. 2012
22242602 Single domain metallothioneins: supermetalation of human MT 1a

Sutherland, DE, Willans, MJ, Stillman, MJ

J. Am. Chem. Soc. 2012
17388808 Evidence for noncooperative metal binding to the alpha domain of human metallothionein

Rigby Duncan, KE, Stillman, MJ

FEBS J. 2007
Participant Of
Inferred From
Orthologous Events