MT2A binds copper

Stable Identifier
R-HSA-5662986
Type
Reaction [binding]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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MT2A binds copper
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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
20463663 Affinity gradients drive copper to cellular destinations

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

Nature 2010
20711450 The native copper- and zinc-binding protein metallothionein blocks copper-mediated Abeta aggregation and toxicity in rat cortical neurons

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

PLoS ONE 2010
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Orthologous Events
MT2A binds copper (Bos taurus)
MT2A binds copper (Canis familiaris)
MT2A binds copper (Danio rerio)
MT2A binds copper (Gallus gallus)
MT2A binds copper (Mus musculus)
MT2A binds copper (Rattus norvegicus)
MT2A binds copper (Sus scrofa)
Authored
May, B  (2015-01-13)
Reviewed
Atrian, S  (2015-09-19)
Created
May, B  (2015-01-14)
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