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Article Abstract
Calmodulin (CaM) binds to the membrane-proximal cytosolic C-terminal domain of Ca 1.2 (residues 1520-1669, CT(1520-1669)) and causes Ca -induced conformational changes that promote Ca -dependent channel inactivation (CDI). We report biophysical studies that probe the structural interaction between CT(1520-1669) and CaM. The recombinantly expressed CT(1520-1669) is insoluble, but can be solubilized in the presence of Ca -saturated CaM (Ca /CaM), but not in the presence of Ca -free CaM (apoCaM). We show that half-calcified CaM (Ca /CaM ) forms a complex with CT(1520-1669) that is less soluble than CT(1520-1669) bound to Ca /CaM. The NMR spectrum of CT(1520-1669) reveals spectral differences caused by the binding of Ca /CaM versus Ca /CaM, suggesting that the binding of Ca to the CaM N-lobe may induce a conformational change in CT(1520-1669).
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9719739 | PMC |
| http://dx.doi.org/10.1002/1873-3468.14529 | DOI Listing |
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