Transport-linked conformational changes in Na,K-ATPase. Structure-function relationships of ligand binding and E1-E2 conformational transitions.
Jorgensen
P L
PL
Biomembrane Research Centre, August Krogh Institute, Copenhagen University, Denmark. PLJORGENSE@aki.ku.dk
Rasmussen
J H
JH
Nielsen
J M
JM
Pedersen
P A
PA
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001224:Aspartic Acid; D001665:Binding Sites; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism*; D013552:Swine
D008024:Ligands; D011994:Recombinant Proteins; D001224:Aspartic Acid; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase