Protein-protein docking study
With the availability of the hs CENP-M crystal structure (PDB 4P0T) and having successfully generated high quality models for each component of the hs CENP-HIK complex, we proceeded with the docking of the subunits. According to the Hu et al . [14] model, biochemical analysis and structures revealed that theth CENP-K and th CENP-H form a heterodimer via interactions at both N-terminal and C-terminal. The integration ofct CENP-INT into the complex is through its interaction with the th CENP-H C-terminal, resulting in the formation of a ternary complex where th CENP-H is sandwiched between ct CENP-INT and th CENP-K [14]. The study also reported the conservation of this architecture in the human HIK complex. Upon the stepwise docking of each generated model of the hs CENP-H, -I, and -K, the resulting output showed a similar architecture with the experimental reports from literature, suggesting a structural conservation across the species (Figure 5).