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Troponin structure and function: a view of recent progress.

Steven B MarstonJuan Eiros Zamora
Published in: Journal of muscle research and cell motility (2019)
The molecular mechanism by which Ca2+ binding and phosphorylation regulate muscle contraction through Troponin is not yet fully understood. Revealing the differences between the relaxed and active structure of cTn, as well as the conformational changes that follow phosphorylation has remained a challenge for structural biologists over the years. Here we review the current understanding of how Ca2+, phosphorylation and disease-causing mutations affect the structure and dynamics of troponin to regulate the thin filament based on electron microscopy, X-ray diffraction, NMR and molecular dynamics methodologies.
Keyphrases
  • molecular dynamics
  • electron microscopy
  • protein kinase
  • density functional theory
  • high resolution
  • magnetic resonance
  • skeletal muscle
  • single molecule
  • mass spectrometry
  • binding protein
  • dna binding