Crystal structures of tropomyosin: flexible coiled-coil.

@article{Nitanai2007CrystalSO,
  title={Crystal structures of tropomyosin: flexible coiled-coil.},
  author={Yasushi Nitanai and Shiho Minakata and Kayo Ma{\'e}da and Naoko Oda and Yuichiro Ma{\'e}da},
  journal={Advances in experimental medicine and biology},
  year={2007},
  volume={592},
  pages={
          137-51
        }
}
Tropomyosin (Tm) is a 400 angstroms long coiled coil protein, and with troponin it regulates contraction in skeletal and cardiac muscles in a [Ca2+]-dependent manner. Tm consists of multiple domains with diverse stabilities in the coiled coil form, thus providing Tm with dynamic flexibility. This flexibility must play important roles in the actin binding and the cooperative transition between the calcium regulated states of the entire muscle thin filament. In order to understand the flexibility… CONTINUE READING

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