[Concepts of the oligomeric structure and function of Na, K-ATPase based on the results of studying ligand binding and of determining the size of the molecular target].
This review is devoted to the discussion of the sizes and molecular structure of the minimal functional unit of Na, K-ATPase. Special attention is paid to the data obtained by radiation inactivation method and studies on ligand binding. The model for the stepwise radiation inactivation of Na, K-ATPase is proposed. The conclusion is drawn that Na, K-ATPase has a dimeric structure, the interactions between its alpha-subunits stabilize the quaternary structure of the pump. Functionally, each alpha-subunit in a stabilized structure possesses a full hydrolytic activity.
Norby
J G
JG
D000818:Animals; D008024:Ligands; D046911:Macromolecular Substances; D008958:Models, Molecular; D015221:Potassium Channels / Q000201:enzymology; D011869:Radioligand Assay; D015222:Sodium Channels / Q000201:enzymology; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
D008024:Ligands; D046911:Macromolecular Substances; D015221:Potassium Channels; D015222:Sodium Channels; D000254:Sodium-Potassium-Exchanging ATPase
Predstavleniia ob oligomernoĭ strukture i funktsii Na, K-ATFazy, osnovannye na rezul'tatakh izucheniia sviazyvaniia ligandov i opredeleniia razmerov molekuliarnoĭ misheni.