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Background: Interleukin-10 is an important anti-inflammatory cytokine that plays significant roles in auto immune diseases. Interleukin-10 has been involved as an important regulator of the functions of myeloid cells lymphoid cells. The three-Dimensional structure and functions of Interleukin-10, proteins from different species are not known. In the present study, we analyzed the comparative study of 3D structure of eight different species of Interleukin-10 proteins and also molecular docking studies were performed to all the modelled structures. Methods: Comparative modelling was performed to all the selected eight proteins by using Modeller 9.21, a modelling tool. Initial alignment was performed by using clustal X and validated by using Procheck. Further molecular docking study was performed by using Autodock 4.2. Results and Discussion: Homology modeling studies of all the modelled proteins showed that all the amino acid residues present in core region and there is no amino acid residue in disallowed region. A molecular docking study was also carried out to study the stability of Interleukin-10 proteins. Docking studies were performed by using natural compounds as Interleukin-10 protein inhibitors. All the compounds exhibited good binding energies and good interactions. Binding energies ranged from -4.51 to -9.82 Kcal/mol. Conclusion: Homology modelling and docking study results indicate that the natural compounds are showing good interactions with all the modelled interleukin-10 proteins. To this study we get significant information for the design of novel inhibitors for the treatment of inflammation.

Homology Modelling and Molecular Docking Studies of Interleukin 10 Proteins from Different Species