Structural analysis of smooth muscle tropomyosin α and β isoforms.

@article{Rao2012StructuralAO,
  title={Structural analysis of smooth muscle tropomyosin α and β isoforms.},
  author={Jampani Nageswara Rao and Roland F Rivera-Santiago and Xiaochuan Edward Li and William Lehman and Roberto Dom{\'i}nguez},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 5},
  pages={3165-74}
}
A large number of tropomyosin (Tm) isoforms function as gatekeepers of the actin filament, controlling the spatiotemporal access of actin-binding proteins to specialized actin networks. Residues ∼40-80 vary significantly among Tm isoforms, but the impact of sequence variation on Tm structure and interactions with actin is poorly understood, because… CONTINUE READING