Literature summary for 7.2.2.13 extracted from

Yatime, L.; Laursen, M.; Morth, J.P.; Esmann, M.; Nissen, P.; Fedosova, N.U.
Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase (2011), J. Struct. Biol., 174, 296-306.

Crystallization (Commentary)

Crystallization (Comment)	Organism
4.6 A resolution crystal structure in its phosphorylated form stabilized by high affinity binding of ouabain. Ouabain binds to a site formed at transmembrane segments alphaM1-alphaM6, plugging the ion pathway from the extracellular side. The A domain has rotated in response to phosphorylation and alphaM1-2 move towards the ouabain molecule, providing for high affinity interactions and closing the ion pathway from the extracellular side	Sus scrofa

Crystallization (Comment)

Organism

4.6 A resolution crystal structure in its phosphorylated form stabilized by high affinity binding of ouabain. Ouabain binds to a site formed at transmembrane segments alphaM1-alphaM6, plugging the ion pathway from the extracellular side. The A domain has rotated in response to phosphorylation and alphaM1-2 move towards the ouabain molecule, providing for high affinity interactions and closing the ion pathway from the extracellular side

Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	P05024	alpha-subunit	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
kidney	-	Sus scrofa	-

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Release 2023.1 (January 2023)