Extended Data Fig. 2: Analysis of the closed conformation of the Mis12C heads.
From: Structure of the human KMN complex and implications for regulation of its assembly
![Extended Data Fig. 2](https://cdn.statically.io/img/media.springernature.com/full/springer-static/esm/art%3A10.1038%2Fs41594-024-01230-9/MediaObjects/41594_2024_1230_Fig9_ESM.jpg)
(a) Comparison of the closed conformation of the heads observed in this study and the open conformation of the heads observed in a previous crystal structure of the complex of Mis12C with CENP-C (PDB 5LSK; ref. 1). In the central superposition, the movement that sways the head2 out of position is marked by a black arrow. The red arrowheads indicate an outward movement of the helices lining the cleft that separates the DSN1 and MIS12 helices when CENP-C binds. (b) AF2 model of the interface between a positively-charged regulatory loop of DSN1 and the negatively charged head1 domain (with contributions from NSL1 and DSN1 in head2).