α- and β-Tubulin Lattice of the Axonemal Microtubule Doublet and Binding Proteins Revealed by Single Particle Cryo-Electron Microscopy and Tomography.

@article{Maheshwari2015A,
  title={α- and β-Tubulin Lattice of the Axonemal Microtubule Doublet and Binding Proteins Revealed by Single Particle Cryo-Electron Microscopy and Tomography.},
  author={Aditi Maheshwari and Jagan M Obbineni and Khanh Huy Bui and Keitaro Shibata and Yoko Yano Toyoshima and Takashi Ishikawa},
  journal={Structure},
  year={2015},
  volume={23 9},
  pages={1584-1595}
}
Microtubule doublet (MTD) is the main skeleton of cilia/flagella. Many proteins, such as dyneins and radial spokes, bind to MTD, and generate or regulate force. While the structure of the reconstituted microtubule has been solved at atomic resolution, nature of the axonemal MTD is still unclear. There are a few hypotheses of the lattice arrangement of its α- and β-tubulins, but it has not been described how dyneins and radial spokes bind to MTD. In this study, we analyzed the three-dimensional… CONTINUE READING
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