The results of site-directed mutagenesis studies of the sarcoplasmic reticulum Ca2+-ATPase are reviewed. More than 250 different point mutants have been expressed in cell culture and analysed by a panel of functional assays. Thereby, 40–50 important amino acid residues have been pinpointed, and the mutants have been assigned to functional classes: the Ca2+-affinity mutants, the phosphorylation-negative mutants, the ATP-affinity mutants, the E1P mutants, the E2P mutants, and the uncoupled mutants. Moreover, regions important to the specific inhibition by thapsigargin have been identified by analysis of Ca2+-ATPase/Na+, K+-ATPase chimeric constructs.
Review Article| October 01 1995
Dissection of the functional domains of the sarcoplasmic reticulum Ca2+-ATPase by site-directed mutagenesis
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Jens Peter Andersen; Dissection of the functional domains of the sarcoplasmic reticulum Ca2+-ATPase by site-directed mutagenesis. Biosci Rep 1 October 1995; 15 (5): 243–261. doi: https://doi.org/10.1007/BF01788358
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