Constraints on models for the folding of the Na,K-ATPase.
We have attempted to bring together in graphic fashion the available evidence on the structure of the Na,K-ATPase and the H,K-ATPase. There appears to be much room for modification of the existing models for transmembrane folding. More sites on each side of the membrane need to be identified. Whether these will be antibody epitopes, sites of covalent modification, or tags inserted by mutagenesis is less important than that there be many of them and that each be verified by alternative approaches. If any single principle has emerged from the study of the topography of membrane proteins, it is that it is easy to reach conclusions too soon.
Sweadner
K J
KJ
Neurosurgical Research, Massachusetts General Hospital, Boston 02114.
Arystarkhova
E
E
D000595:Amino Acid Sequence; D000818:Animals; D001666:Binding Sites, Antibody; D000252:Calcium-Transporting ATPases / Q000737:chemistry; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D000939:Epitopes / Q000032:analysis; D017506:H(+)-K(+)-Exchanging ATPase / Q000737:chemistry*; D008961:Models, Structural; D008969:Molecular Sequence Data; D017510:Protein Folding; D051381:Rats; D017386:Sequence Homology, Amino Acid; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry*
D000939:Epitopes; D017506:H(+)-K(+)-Exchanging ATPase; D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase