Docking Troponin T onto the Tropomyosin Overlapping Domain of Thin Filaments.

ABSTRACT: Complete description of thin filament conformational transitions accompanying muscle regulation requires ready access to atomic structures of actin-bound tropomyosin-troponin. To date, several molecular-docking protocols have been employed to identify troponin interactions on actin-tropomyosin because high-resolution experimentally determined structures of filament-associated troponin are not available. However, previously published all-atom models of the thin filament show chain separation and corruption of components during our molecular dynamics simulations of the models, implying artifactual subunit organization, possibly due to incorporation of unorthodox tropomyosin-TnT crystal structures and complex FRET measurements during model construction. For example, the recent Williams et al.

SUBMITTER: Pavadai E 

PROVIDER: S-EPMC6976810 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature