Sandbox Reserved 811: Difference between revisions
Katja Rueger (talk | contribs) No edit summary |
Katja Rueger (talk | contribs) No edit summary |
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It is the catalytic component of the enzyme. It has binding domains for ATP and the cations. So it catalyzes the hydrolysis of ATP into ADP and permits the exchange of Na+ and K+. | It is the catalytic component of the enzyme. It has binding domains for ATP and the cations. So it catalyzes the hydrolysis of ATP into ADP and permits the exchange of Na+ and K+. | ||
The α-subunit has three highly-conserved domains: the actuator domain (A), the nucleotide-binding domain (N) and the phosphorylation domain (P). Their conformation changes in response to ligand binding that allows ion exchange across the membrane. | The α-subunit has three highly-conserved domains: the actuator domain (A), the nucleotide-binding domain (N) and the phosphorylation domain (P). Their conformation changes in response to ligand binding that allows ion exchange across the membrane. | ||
[[Image:3B8E 2D view.jpg|thumb|Architecture of the Na+,K+-ATPase αβγ-complex, with its K+/Rb+ sites.|450px]] | |||
== Fixation of cations == | == Fixation of cations == | ||