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).