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

Fig. 4. Homology-based model of the D. melanogaster augmin complex.

Fig. 4

a The structures of all six possible D. melanogaster T-III subcomplexes (top) and possible T-II subcomplexes (bottom) were predicted by AlphaFold2-Multimer. Structures that superimpose with X. laevis T-II or T-III are circled. By categorizing the resulting predictions, Dgt2 and Wac were found to bind consistently with T-III subunits Dgt3 and Dgt5, as well as dimerizing with one another, and, similarly, Msd1 and Msd5 consistently dimerized with one another and bound T-II subunits Dgt4 and Dgt6. b Structural alignment of the D. melanogaster subcomplexes T-II and T-III resulted in a molecular model of D. melanogaster augmin. The γ-TuRC adaptor protein GCP71WD (aka NEDD1)35, has been demonstrated to bind to the heterodimer of Dgt31–350 and Dgt51–450, and that span of residues, comprising the likely NEDD1 binding site, have been annotated.