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- W2790674612 abstract "We have used a combination of site-directed spin labeling and EPR spectroscopy to probe the interaction of calmodulin (CaM) with a peptide (RyRp) corresponding to the CaM-binding site on the ryanodine receptor (RYR), the muscle calcium release channel. A bifunctional spin label (BSL) attached stereospecifically at Cys sites i and i+4 was used to label CaM at positions 34 and 38 in the N-lobe and 106 and 110 in the C-lobe. TOAC, an unnatural paramagnetic amino acid, was used to label RyRp at position 5. Interspin CaM-CaM distances measured by DEER indicated that CaM, in the absence of peptide and Ca, exists predominantly in a closed conformation (short interspin distance), while Ca induces a shift in equilibrium toward two additional conformations, one more open and another more closed (“compact”). Addition of unlabeled RyRp decreased the distance, indicating that the two lobes of CaM collapse toward each other (compact conformation). Removal of Ca increased the distance between the spin labels, indicating greater lobe separation. Intermolecular distances measured between BSL (on CaM) and TOAC (on RyRp) revealed that in the absence of Ca, the complex is structurally heterogeneous, as evidenced by multiple populations in the distance distribution. Addition of calcium induced a shift toward a single compact structure. This effect was more significant with BSL on the N- lobe than on the C-lobe, suggesting that the N-lobe of CaM functions as the main Ca-sensor in regulating RyR. These results provide insight into the structural dynamics of the Ca-dependent regulation of RyR by CaM. These studies are currently being extended to investigate the effect of CaM mutation and oxidation. This work was supported by NIH grants to DDT (R37 AG26160, T32 AR007612)." @default.
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- W2790674612 date "2018-02-01" @default.
- W2790674612 modified "2023-09-30" @default.
- W2790674612 title "Probing the Calcium-Dependent Structural States of Calmodulin-RyR using Bifunctional Spin Labels and Deer" @default.
- W2790674612 doi "https://doi.org/10.1016/j.bpj.2017.11.890" @default.
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