Fig. 6: Model of the MIS12-CSM1 interface.
From: The composition and structure of the outer kinetochore KMN complex is conserved across kingdoms
A Structural model obtained using AlphaFold3 of the complex between the MIS12 module and the Csm1 homodimer in A. thaliana mediated by the N-terminal tail of Dsn1 (red). B The structural model generated by AlphaFold3 for the homologous complex in S. cerevisiae exhibits a different binding mode with respect to A. thaliana consistent with the bound conformation observed in the experiment X-ray structure of a closely related complex Plowman et al.20 of note, there is no detected homolog of Csm1 in H. sapiens. C Structural model generated by AlphaFold3 of the complex between the MIS12 module and the CENPC N-terminal disordered tail (brown color) in three species. In all cases, the region predicted with low PAE (higher confidence) corresponds to a short stretch of CENPC binding to the two-helix head of Mis12 subunit. The region of CENPC predicted for H. sapiens and S. cerevisiae is the same as the one identified experimentally and adopts a very similar conformation to that observed in the X-ray structure.
