Figure 1

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TbKINX1B is an N-kinesin with a classical motor domain. A. Predicted secondary structure representation of TbKINX1B protein. The kinesin motor domain (TbKINX1BMD aa. 4-496 with P-loop aa. GQTGSGKT, Switch I aa. NEHSSRSH and Switch II aa. DLAGSE), TbKINX1B leucine zipper (LZ, aa. 756–784), the coiled-coil (aa. 1082–1297), and the TbBILBO1-binding domain (B1BD aa. 517–715) are shown. B. Alignment-based homology model of TbKINX1B motor domain to Mus musculus KIF1A motor domain (PDB 1I5S) by Phyre2 software. The predicted tertiary structure is represented as a superposition of both kinesin motor domains, TbKINX1B (colored: yellow for β-sheet and red for α-helix) and KIF1A (white), corresponding to 100% match. C. Western blot analysis of TbKINX1B in PCF and BSF cells. TbKINX1B, TbBILBO1 and Tubulin were probed on whole cells (WC), detergent-extracted cytoskeleton (CSK) and soluble fraction (S) of lysed cells.
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