Lysine 480 is not an essential residue for ATP binding or hydrolysis by Na,K-ATPase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+,K+- and other cation transport ATPases.
2. Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA
3. Amino-acid sequence of a Ca2+ + Mg2+ -dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
4. Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases
5. Molecular cloning of the rat stomach (H+ + K+)-ATPase.
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3. The Crystallographic Structure of Na,K-ATPase N-domain at 2.6Å Resolution;Journal of Molecular Biology;2003-10
4. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase;Nature Structural & Molecular Biology;2003-05-05
5. Replacement of Several Single Amino Acid Side Chains Exposed to the Inside of the ATP-binding Pocket Induces Different Extents of Affinity Change in the High and Low Affinity ATP-binding Sites of Rat Na/K-ATPase;Journal of Biological Chemistry;2002-10
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