Figure 5. Cartoon and surface representation of the (A) fungal (PDB 5Z08), (B) yeast (PDB 6YPC), and (C) human model of the CENP-HIK structural architecture. All CENP-H (th CENP-H184-227,sc CENP-H147-181, andhs CENP-H194-247) are sandwiched between CENP-I (ct CENP-I8-229,sc CENP-I2-241, andhs CENP-I1-265) and CENP-K (th CENP-K161-328,sc CENP-K136-237, andhs CENP-K161-269). The blue, green and pale yellow colors denote CENP-H, CENP-K and CENP-I respectively for all species.
In a similar study, Basilico et al. [37] reported the structural organization of the hs CENP-HIKM complex, using a computational model to represent the full length hs CENP-I as there existed no full length ortholog of the protein. Consistent with existing literature reports, the molecular docking output also showed that the hs CENP-M binds to the C-terminal of the full lengthhs CENP-I model (Figure 5) in an appearance that resembles the importin-β/Ran complex as reported by Basilico et al . [37]. The α-solenoid fold of importin-β is consistently reported to be a high-confidence hs CENP-I structural modeling template [37].