Single mutation of Lys or Arg residue in ATP binding pocket in rat Na/K-ATPase alpha-1 subunit induces different affinity change in high- and low-affinity ATP binding.
Imagawa
Toshiaki
T
Biological Chemistry, Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan. toshi@sci.hokudai.ac.jp
Teramachi
Satomi
S
Taniguchi
Kazuya
K
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001120:Arginine; D001665:Binding Sites; D018360:Crystallography, X-Ray; D007700:Kinetics; D008239:Lysine; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism*
D021122:Protein Subunits; D000255:Adenosine Triphosphate; D001120:Arginine; D000254:Sodium-Potassium-Exchanging ATPase; D008239:Lysine