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. 2023 Apr 13;14:2072. doi: 10.1038/s41467-023-37519-4

Fig. 5. Interaction of augmin complex with the microtubule and other cellular factors.

Fig. 5

a Augmin T-II, centered on the calponin homology of Haus6, is displayed as a surface colored by electrostatics (where red is electronegative, and blue is electropositive). A single tubulin dimer, positioned as it would be if bound to the CH domain of NDC80, is displayed in cartoon form (light gray, α-tubulin; dark gray, β-tubulin). b Similar to a, except that the surface of augmin T-II is colored by amino acid conservation (where purple is conserved and white is variable). c Overview of updated model of the MT branch site, including augmin molecular model. The NEDD1 γ-TuRC adaptor binding site is predicted to be located within T-III and/or the C-terminus of Haus6 (green line). Two MT binding site are predicted within T-II, one within the disordered MTBD of Haus8 (yellow line), and a second within the CH domain of Haus6.