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This study proposes a kinetic model explaining how phospholamban binding decreases the apparent affinity of Ca2+-ATPase for Ca2+ via two binding modes.
Binding of phospholamban (PLN) to the Ca(2+)-ATPase of muscle sarcoplasmic reticulum results in a decrease in apparent affinity for Ca(2+) without affecting the true binding constant for Ca(2+) determined in equilibrium binding experiments. It is shown that this can be explained by a scheme in which the ATPase shows two modes of binding for PLN, one of high and one of low affinity; the proposed scheme is not dependent on the kinetic model assumed for the Ca(2+)-ATPase.
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Anthony G. Lee (2003) studied this question.
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