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. 2018 Mar 6;37(8):e97902. doi: 10.15252/embj.201797902

Figure 5. Crystal structure of ClACCp.

Figure 5

  1. Schematic illustration of CHC (grey) and TACC3 (orange) domain structures.
  2. Summary of the binding data between CHC proteins and TACC3CID peptides. See also panel (G) and Fig EV5A and B.
  3. FP assays to measure the binding affinity of CHC 1–574 to FAM‐labelled TACC3CID phosphorylated (pS558), unphosphorylated (S558) and phosphomimetic (S558E) forms. See also Fig EV5C.
  4. Overview of the crystal structure of ClACCp. Note that the linker between CHC aa574 and TACC3 aa550 is disordered.
  5. Magnified view of the CHC/TACC3 interaction. The side chains of key interacting residues are shown as sticks.
  6. Schematic illustration of the CHC/TACC3 interface.
  7. FP binding curves of CHC 1–574 with FAM‐phospho‐TACC3CID bearing alanine point mutations. Affinities are in parentheses. Data represent mean of three experiments ± SD.