MT2A binds copper

Stable Identifier
Reaction [binding]
Homo sapiens
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The metallothionein MT2A binds 10 atoms of copper(I). Complexes with up to 12 atoms of Cu+ are observed, however the predominant form appears to be MT2A:10Cu+ (Banci et al. 2010, Chung et al. 2010). Metallothioneins and CuZn-SOD have the highest affinities of cellular proteins for copper(I), but metallothioneins are incapable of removing copper from other cellular enzymes (Banci et al. 2010).

Literature References
PubMed ID Title Journal Year
20711450 The native copper- and zinc-binding protein metallothionein blocks copper-mediated Abeta aggregation and toxicity in rat cortical neurons

Chung, RS, Howells, C, Eaton, ED, Shabala, L, Zovo, K, Palumaa, P, Sillard, R, Woodhouse, A, Bennett, WR, Ray, S, Vickers, JC, West, AK

PLoS ONE 2010
20463663 Affinity gradients drive copper to cellular destinations

Banci, L, Bertini, I, Ciofi-Baffoni, S, Kozyreva, T, Zovo, K, Palumaa, P

Nature 2010
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Orthologous Events