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- W4225696643 abstract "Calmodulin (CaM) is a calcium-binding protein that regulates the function of many proteins by indirectly conferring Ca2+ sensitivity, and it undergoes a large conformational change on partners' binding. We compared the solution binding mode of the target peptides MARCKS and IQ by double electron-electron resonance (DEER) distance measurements and paramagnetic NMR. We combined nitroxide and Gd(III) spin labels, including specific substitution of one of the Ca2+ ions in the CaM mutant N60D by a Gd(III) ion. The binding of MARCKS to holo-CaM resulted neither in a closed conformation nor in a unique relative orientation between the two CaM domains, in contrast with the crystal structure. Binding of IQ to holo-CaM did generate a closed conformation. Using elastic network modeling and 12 distance restraints obtained from multiple holo-CaM/IQ DEER data, we derived a model of the solution structure, which is in reasonable agreement with the crystal structure." @default.
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- W4225696643 date "2022-06-01" @default.
- W4225696643 modified "2023-09-27" @default.
- W4225696643 title "DEER experiments reveal fundamental differences between calmodulin complexes with IQ and MARCKS peptides in solution" @default.
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- W4225696643 doi "https://doi.org/10.1016/j.str.2022.03.005" @default.
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