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Site-directed mutagenesis studies of the sarcoplasmic reticulum Ca 2+ -ATPase have pinpointed five amino acid residues that are essential to Ca 2+ occlusion, and these residues have been assigned to different parts of a Ca 2+ binding pocket with channel-like structure. Three of the homologous Na + ,K + -ATPase residues have been shown to be important...
The glutamic acid residue Glu 771 in the fifth transmembrane segment M5 of the Ca 2+ -ATPase of rabbit fast twitch muscle sarcoplasmic reticulum was substituted with lysine, alanine, and glycine by site-directed mutagenesis. Mutant Glu 771 ->Lys was unable to occlude Ca 2+ , and Ca 2+ did not inhibit phosphorylation from...
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