Key result
Structural and dynamic studies of Ca2+ and Mg2+ binding to the cytosolic domains CBD1 and CBD2 enhance the understanding of Na+/Ca2+ exchanger regulation.
This review provides a structural perspective on how intracellular calcium and magnesium regulate the Na+/Ca2+ exchanger via its cytosolic binding domains.
No immediate clinical implications for NCX modulation; leaves open translation of CBD binding insights to therapeutic development.
Intracellular Ca2+ regulates the activity of the NCX (Na+/Ca2+ exchanger) through binding to the cytosolic CBD (Ca2+-binding domain) 1 and CBD2. In vitro studies of the structure and dynamics of CBD1 and CBD2, as well as studies of their kinetics and thermodynamics of Ca2+ binding, greatly enhanced our understanding of NCX regulation. We describe the fold of the CBDs in relation to other known structures and review Ca2+ binding of the different CBD variants from a structural perspective. We also report on new findings concerning Mg2+ binding to the CBDs and finally we discuss recent results on CBD1-CBD2 interdomain interactions.
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Breukels et al. (2012) conducted a review in Na+/Ca2+ exchanger regulation. Structural and dynamic studies of Ca2+ and Mg2+ binding to the cytosolic domains CBD1 and CBD2 enhance the understanding of Na+/Ca2+ exchanger regulation.
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