Literature summary for 7.2.2.9 extracted from

Tsay, M.J.; Fatemi, N.; Narindrasorasak, S.; Forbes, J.R.; Sarkar, B.
Identification of the "missing domain" of the rat copper-transporting ATPase, atp7b: insight into the structural and metal binding characteristics of its N-terminal copper-binding domain (2004), Biochim. Biophys. Acta, 1688, 78-85.

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Cloned(Commentary)

Cloned (Comment)	Organism
cloning of the DNA segment coding for the N-terminal copper-binding region into a GST pGEX-6P-2 vector	Rattus norvegicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu+	the metal-dependent conformational changes observed in the N-terminal region of the ATPase may not require the presence of the CXXC motif on every domain, as long as the domain has the proper shape, which is an heavy metal-associated-domain-like fold, and as long as some of them contain the CXXC metal binding site. At a certain point during the cooperative binding of Cu(I), protein/protein interactions among the heavy metal-associated -domains begin to dominate the conformational changes in rat ATP7B, while metal binding to the heavy metal-associated -domains makes a smaller contribution	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	Q64535	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
ATP7B	-	Rattus norvegicus
copper-transporting ATPase	-	Rattus norvegicus

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Release 2023.1 (January 2023)