Key result
The crystal structure of the C-terminal 31 residues of striated-muscle α-tropomyosin reveals a splayed α-helical conformation that forms a specific recognition site for troponin T.
Population
Recombinant protein of the C-terminal 31 residues of rat striated-muscle alpha-tropomyosin preceded by a…
Design
Preclinical
Authors
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Structural insight into thin-filament regulation; hypothesis-generating for cardiac muscle disorders and requires human validation before clinical consideration.
The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a splayed conformation that serves as a specific recognition site for troponin T, clarifying the physical basis for striated muscle regulation.
Li et al. (2002) studied this question. X-ray crystallography of GCN4-CTm chimeric peptide was evaluated on Crystal structure determination at 2.7 Å resolution. The crystal structure of the C-terminal 31 residues of striated-muscle α-tropomyosin reveals a splayed α-helical conformation that forms a specific recognition site for troponin T.