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Selenocysteine Positional Variants Reveal Contributions to Copper Binding from Cysteine Residues in Domains 2 and 3 of Human Copper Chaperone for Superoxide Dismutase

The human copper chaperone for superoxide dismutase binds copper both in an Atx1-like MTCQSC motif in domain 1, and via a multinuclear cluster formed by two CXC motifs at the D3 dimer interface. The composition of the Cu(I) cluster has been investigated previously by mutagenesis of the CXC motif, an...

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Bibliografiset tiedot
Päätekijät: Barry, Amanda N., Clark, Kevin M., Otoikhian, Adenike, van der Donk, Wilfred A., Blackburn, Ninian J.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2008
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Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC2645929/
https://ncbi.nlm.nih.gov/pubmed/19007184
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi801438g
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