Myostatin (MSTN) belongs to the growth factor (TGF-β) family, which is mainly produced by muscle cells, which inhibits the growth of muscle mass. Activins regulate the growth and differentiation of variety of cell types. Follistatin antagonizes the action of TGF-β ligands, such as MSTN and activin A. Recombinant follistatin protein improves skeletal muscle healing after injury and disease through an interaction with muscle regeneration. Therefore, the aim of this study is to predict the three-dimensional structure of human MSTN and investigate the interaction between MSTN and equine follistatin by molecular docking method. The human MSTN structure was predicted with the SWISS MODEL server and evaluated with SAVES 6.0 online server. Then, the interactions of human MSTN with equine follistatin were performed using the H-DOCK online server based on the combined algorithm of template-based modeling and ab-initio free docking. Examination of ERRAT, Ramachandran plot and Z-SCORE showed that the prediction of two constructs was done successfully. The results of molecular docking also showed that the two studied proteins are connected to each other in a suitable position with a high confidence score of 0.7. The results of this study indicated the potential utility of equine follistatin to inhibit human MSTN, although further molecular dynamics studies are needed in addition to in vitro experiments.

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