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.