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Literature summary for 7.2.2.9 extracted from

  • Banci, L.; Bertini, I.; Cantini, F.; DellaMalva, N.; Herrmann, T.; Rosato, A.; Wüthrich, K.
    Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein (2006), J. Biol. Chem., 281, 29141-29147.
    View publication on PubMed
Search for more literature for 7.2.2.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of the DNA sequence encoding MNK3, corresponding to amino acids 275-352 of ATP7A in Escherichia coli strain BL21 (DE3)pLysS. Introduction of a C-terminal expression tag including His6 to ease purification Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Cu+ structural characterization of the apo- and copper(I)-form of the third domain of ATP7A. Investigation of the interaction of MNK3 (the third metal-binding domain, a copper(I)-transporrting ATPase) with the partner human protein HAH1. MNK3 is the most differentiated metal-binding domain in ATP7A. Metallation of MNK3 could be an event quite suited to signal high intracellular copper(I) concentration and could trigger the appropriate response Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q04656
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
ATP7A
-
 Homo sapiens
Menkes disease protein
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 Homo sapiens