Conclusion
With the aid of extensive computational approaches and following experimentally validated site-directed mutagenesis from literature reports, we have designed an hypothetical model of thehs CENP-HIKM complex. Structurally refined models of each subunit were individually docked to generate an hypothetical complex which was subjected to several in silico protocols such as, the normal mode analysis, in silico mutagenesis, binding free energy prediction upon mutation, and analysis of the non-covalent interactions, in an attempt to validate the model reliability. Knowledge of thehs CENP-HIKM architecture and the surface residues at the interaction site as presented in this study may provide more insight into the mechanisms of abnormal interactions in disease states, through the comprehension of simple molecular recognition mechanisms. Such information may present future therapeutic potentials for rational development of drugs that regulate or mimic the effects of protein-protein interactions.