Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling

@article{Lu2015StructureOM,
  title={Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling},
  author={Q. Lu and Jianchao Li and F. Ye and Mingjie Zhang},
  journal={Nature Structural \&Molecular Biology},
  year={2015},
  volume={22},
  pages={81-88}
}
Class I myosins can sense cellular mechanical forces and function as tension-sensitive anchors or transporters. How mechanical load is transduced from the membrane-binding tail to the force-generating head in myosin-1 is unknown. Here we determined the crystal structure of the entire tail of mouse myosin-1c in complex with apocalmodulin, showing that myosin-1c adopts a stable monomer conformation suited for force transduction. The lever-arm helix and the C-terminal extended PH domain of the… Expand
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