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- W2009737112 abstract "The Troponin (Tn) molecular switch contains highly dynamic regions which allow for Ca2+ induced conformational changes to be propagated through to the thin filament. The Mobile domain (Md) of TnI, a secondary thin filament binding domain, is a key player in this process. The functional importance of the Md is also highlighted through the clustering of cardiomyopathy mutations. Structural elucidation of this region by traditional methods is often limited by the absence of key thin filament binding partners. Current Md models describe a highly dynamic region with either a nascent or a well-defined structure. We have utilized Site-Directed Spin Labeling Electron Paramagnetic Resonance (SDSL-EPR) to elucidate the structure of the Md upon interaction with the thin filament. EPR mobility measurements from cysteine scanning of the Md (res. 175-206) in the reconstituted thin filament show a highly dynamic domain in the +Ca2+ (ON) state. A decrease in the mobility occurs in the -Ca2+ (OFF) state, indicating interaction with the thin filament. Further, trends in the mobility of the EPR label reveal two helical structural components within the Md (res. 175-179 & 192-202). Conventional EPR methods were used to measure three interspin distances (176/178, 176/179 & 176/180) which further confirm this assignment. Double Electron-Electron Resonance (DEER) was used to measure the longer interspin distance (178/206) and found that the Md exists in an extended conformation (34±26A). An extended helical structural model for the interaction of the Md with the thin filament through electrostatic bonding is proposed. Residues involved in cardiomyopathy are found clustered at the interacting interface." @default.
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- W2009737112 date "2010-01-01" @default.
- W2009737112 modified "2023-09-28" @default.
- W2009737112 title "Structure and Dynamics of the Mobile Domain of Troponin I by SDSL-EPR" @default.
- W2009737112 doi "https://doi.org/10.1016/j.bpj.2009.12.798" @default.
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