Recent structural biology and molecular dynamics studies have advanced the understanding of how calcium binding, phosphorylation, and disease-causing mutations regulate muscle contraction through conformational changes in the troponin complex.
This review provides a comprehensive overview of the structural and dynamic changes in the troponin complex upon calcium binding and phosphorylation, integrating data from X-ray crystallography, NMR, and molecular dynamics.
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.
Marston et al. (Sat,) conducted a review in Muscle contraction regulation (Troponin structure and function). Recent structural biology and molecular dynamics studies have advanced the understanding of how calcium binding, phosphorylation, and disease-causing mutations regulate muscle contraction through conformational changes in the troponin complex.