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Approximately 50% of the genetic defects of the Na+/K+ pump have been identified in humans. Since the first observation of the carrier defect in familial erythrocytosis in man, more than 40 years ago, there have been many advances in our understanding of the molecular mechanisms underlying this defect. The gene encoding the pump is large and complex. Three alpha-subunits of the pump have been identified to date. Two of these subunits, alpha 1 and alpha 2, are present in all cells except red cells and are the sites of most of the mutations which underlie the carrier syndrome. They are highly hydrophobic and consist of eight membrane spanning domains. Each domain has a single transmembrane helix followed by two short hydrophilic helices on both sides of the membrane. The fifth transmembrane domain is followed by a large hydrophilic loop. The putative pore region of the pump lies within this loop and the residues that most likely form this portion of the channel have been identified by sequence analysis. The third subunit, alpha 3, is a developmentally regulated type II Na+/K+-ATPase specific for the adrenal medulla. Analysis of the alpha 3 mutant responsible for congenital adrenal hyperplasia has shown that this subunit is not essential for Na+/K+ pump activity. alpha 3 appears to