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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...
Tallennettuna:
| Päätekijät: | , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2008
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| Aiheet: | |
| 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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