June 2025
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14 Reads
Revista Brasileira de Ciência Avícola
Follistatin (FST) is a cysteine-rich monomeric protein capable of binding and neutralizing the action of several members of the transforming growth factor-beta (TGFβ) family, such as myostatin and activin, by binding to their receptors. The aim of the present study was to characterize the FST gene and its receptors in quail. Genomic sequences of the FST gene and its receptors in quail were obtained from the National Center for Biotechnology Information (NCBI) database. Analyses of evolutionary relationship, conserved domain, gene structure, and motif pattern of the FST gene family showed the evolutionary conserved nature in quail and other related avian species. Most of the FST proteins are acidic, thermostable, unstable, and hydrophilic in nature, except for FSTL2 and FSTL3, which were basic in nature. A comparative amino acid analysis showed a higher amino acid variation in quail FST genes, as a total of 102 single amino acid changes were identified in all quail FST genes. Mutation analysis showed that 15 mutations had an overall deleterious effect on the structure and functions of the proteins in quail. Molecular docking and Dynamic Simulation (MD) simulation were performed to study dynamics of more promising compounds such as isovitexin, apigetrin, and fleminchaloneto, revealing stability of ligand-protein complex. The values of Root Mean Square Deviation (RMSD), Root Mean Square Fluctuation (RMSF), and results of isovitexin indicated that ligand-protein complex was more compacted than enzymes that are native. This study provides insights into the molecular structure of FST genes in avian species, while exploring the potential of single nucleotide polymorphisms (SNPs) in selective breeding of quail for better performance. Keywords: Follistatin; activin; quail; myostatin; transforming growth factor beta family; molecular docking simulation